HEADER OXIDOREDUCTASE 02-NOV-01 1KAH
TITLE L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINE
TITLE 2 (PRODUCT), ZN AND NAD (COFACTOR)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HDH;
COMPND 5 EC: 1.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: HISD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS L-HISTIDINOL DEHYDROGENASE, HOMODIMER, ROSSMANN FOLD, 4 DOMAINS,
KEYWDS 2 HISD, L-HISTIDINE BIOSYNTHESIS, NAD COFACTOR, ZINC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.R.G.BARBOSA,J.SIVARAMAN,Y.LI,R.LAROCQUE,A.MATTE,J.D.SCHRAG,
AUTHOR 2 M.CYGLER
REVDAT 7 15-NOV-23 1KAH 1 REMARK
REVDAT 6 16-AUG-23 1KAH 1 REMARK SEQADV LINK
REVDAT 5 12-NOV-14 1KAH 1 KEYWDS
REVDAT 4 24-FEB-09 1KAH 1 VERSN
REVDAT 3 11-JUL-06 1KAH 1 AUTHOR JRNL
REVDAT 2 01-APR-03 1KAH 1 JRNL
REVDAT 1 12-JUN-02 1KAH 0
JRNL AUTH J.A.R.G.BARBOSA,J.SIVARAMAN,Y.LI,R.LAROCQUE,A.MATTE,
JRNL AUTH 2 J.D.SCHRAG,M.CYGLER
JRNL TITL MECHANISM OF ACTION AND NAD+-BINDING MODE REVEALED BY THE
JRNL TITL 2 CRYSTAL STRUCTURE OF L-HISTIDINOL DEHYDROGENASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 1859 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11842181
JRNL DOI 10.1073/PNAS.022476199
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 233928.220
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 51340
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2069
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4407
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 172
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6432
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.99000
REMARK 3 B22 (A**2) : -4.02000
REMARK 3 B33 (A**2) : -6.97000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.100 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 35.03
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NAD.PARAM
REMARK 3 PARAMETER FILE 5 : HISTIDINOL.PARAM
REMARK 3 PARAMETER FILE 6 : GLYCEROL.PARAM
REMARK 3 PARAMETER FILE 7 : ACETATE.PARAM
REMARK 3 PARAMETER FILE 8 : DTT.PARAM
REMARK 3 PARAMETER FILE 9 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NAD.TOP
REMARK 3 TOPOLOGY FILE 5 : HISTIDINOL.TOP
REMARK 3 TOPOLOGY FILE 6 : GLYCEROL.TOP
REMARK 3 TOPOLOGY FILE 7 : ACETATE.TOP
REMARK 3 TOPOLOGY FILE 8 : DTT.TOP
REMARK 3 TOPOLOGY FILE 9 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MODEL ONLY PARTIALLY REFINED
REMARK 4
REMARK 4 1KAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014760.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53978
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1K75
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, GLYCEROL, IMIDAZOLE/MALIC
REMARK 280 ACID BUFFER, AMMONIUM SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.63000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.97000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.97000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.63000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.54500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 PHE A 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MSE B 1 CB CG SE CE
REMARK 470 SER B 2 CB OG
REMARK 470 PHE B 3 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 5 99.97 48.29
REMARK 500 SER A 27 -74.39 -94.76
REMARK 500 ALA A 28 16.05 56.40
REMARK 500 SER A 29 128.40 -23.55
REMARK 500 LYS A 57 -76.26 -54.26
REMARK 500 ASP A 59 146.09 76.27
REMARK 500 THR A 61 -35.76 -145.15
REMARK 500 THR A 62 54.21 39.47
REMARK 500 THR A 64 -82.85 -100.31
REMARK 500 ALA A 166 151.05 -48.88
REMARK 500 ASN A 211 -173.30 -61.65
REMARK 500 GLN A 331 72.03 -101.95
REMARK 500 SER A 354 66.14 -117.33
REMARK 500 LEU A 416 79.48 -105.15
REMARK 500 SER B 2 69.24 69.33
REMARK 500 PHE B 3 -167.00 -178.90
REMARK 500 THR B 5 -67.31 -129.42
REMARK 500 SER B 27 -129.36 -77.45
REMARK 500 ALA B 28 -27.64 -168.53
REMARK 500 SER B 29 89.81 42.56
REMARK 500 THR B 64 -82.61 -104.93
REMARK 500 SER B 135 -78.50 -56.32
REMARK 500 MSE B 232 154.85 178.71
REMARK 500 PRO B 293 -74.78 -42.17
REMARK 500 ARG B 294 79.91 -110.44
REMARK 500 GLN B 331 70.09 -105.49
REMARK 500 ASN B 334 44.42 -108.26
REMARK 500 SER B 354 70.81 -118.07
REMARK 500 TYR B 374 -3.20 -58.80
REMARK 500 GLU B 432 -70.60 -51.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HIS A 503
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 262 NE2
REMARK 620 2 ASP A 360 OD2 160.9
REMARK 620 3 HIS A 502 N 71.2 91.3
REMARK 620 4 HIS A 502 ND1 95.9 90.6 86.7
REMARK 620 5 HIS B 419 NE2 93.9 100.1 156.8 113.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 419 NE2
REMARK 620 2 HIS A 503 ND1 115.8
REMARK 620 3 HIS B 262 NE2 95.5 84.8
REMARK 620 4 ASP B 360 OD2 96.6 86.0 167.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HIS A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HIS A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K75 RELATED DB: PDB
REMARK 900 L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE IMPLICATES DOMAIN
REMARK 900 SWAPPING AND GENE DUPLICATION
REMARK 900 RELATED ID: 1KAE RELATED DB: PDB
REMARK 900 L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-
REMARK 900 HISTIDINOL (SUBSTRATE), ZINC AND NAD (COFACTOR)
REMARK 900 RELATED ID: 1KAR RELATED DB: PDB
REMARK 900 L-HISTIDINOL DEHYDROENASE (HISD) STRUCTURE COMPLEXED WITH HISTAMINE
REMARK 900 (INHIBITOR), ZINC AND NAD (COFACTOR)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FOLLOWING FOUR RESIDUES ARE VARIANT IN THE SWISSPROT
REMARK 999 ENTRY P06988. RESIDUE 14 CAN BE EITHER GLU OR VAL,
REMARK 999 RESIDUE 149 CAN BE EITHER SER OR ARG, RESIDUE 312 CAN BE
REMARK 999 EITHER LEU OR SER AND RESIDUE 402 CAN BE EITHER LEU OR VAL.
DBREF 1KAH A 1 434 UNP P06988 HISX_ECOLI 0 433
DBREF 1KAH B 1 434 UNP P06988 HISX_ECOLI 0 433
SEQADV 1KAH MSE A 1 UNP P06988 MET 0 MODIFIED RESIDUE
SEQADV 1KAH GLU A 15 UNP P06988 VAL 14 SEE REMARK 999
SEQADV 1KAH MSE A 22 UNP P06988 MET 21 MODIFIED RESIDUE
SEQADV 1KAH MSE A 88 UNP P06988 MET 87 MODIFIED RESIDUE
SEQADV 1KAH MSE A 144 UNP P06988 MET 143 MODIFIED RESIDUE
SEQADV 1KAH SER A 150 UNP P06988 ARG 149 SEE REMARK 999
SEQADV 1KAH MSE A 232 UNP P06988 MET 231 MODIFIED RESIDUE
SEQADV 1KAH MSE A 277 UNP P06988 MET 276 MODIFIED RESIDUE
SEQADV 1KAH LEU A 313 UNP P06988 SER 312 SEE REMARK 999
SEQADV 1KAH MSE A 390 UNP P06988 MET 389 MODIFIED RESIDUE
SEQADV 1KAH LEU A 403 UNP P06988 VAL 402 SEE REMARK 999
SEQADV 1KAH MSE B 1 UNP P06988 MET 0 MODIFIED RESIDUE
SEQADV 1KAH GLU B 15 UNP P06988 VAL 14 SEE REMARK 999
SEQADV 1KAH MSE B 22 UNP P06988 MET 21 MODIFIED RESIDUE
SEQADV 1KAH MSE B 88 UNP P06988 MET 87 MODIFIED RESIDUE
SEQADV 1KAH MSE B 144 UNP P06988 MET 143 MODIFIED RESIDUE
SEQADV 1KAH SER B 150 UNP P06988 ARG 149 SEE REMARK 999
SEQADV 1KAH MSE B 232 UNP P06988 MET 231 MODIFIED RESIDUE
SEQADV 1KAH MSE B 277 UNP P06988 MET 276 MODIFIED RESIDUE
SEQADV 1KAH LEU B 313 UNP P06988 SER 312 SEE REMARK 999
SEQADV 1KAH MSE B 390 UNP P06988 MET 389 MODIFIED RESIDUE
SEQADV 1KAH LEU B 403 UNP P06988 VAL 402 SEE REMARK 999
SEQRES 1 A 434 MSE SER PHE ASN THR ILE ILE ASP TRP ASN SER CYS THR
SEQRES 2 A 434 ALA GLU GLN GLN ARG GLN LEU LEU MSE ARG PRO ALA ILE
SEQRES 3 A 434 SER ALA SER GLU SER ILE THR ARG THR VAL ASN ASP ILE
SEQRES 4 A 434 LEU ASP ASN VAL LYS ALA ARG GLY ASP GLU ALA LEU ARG
SEQRES 5 A 434 GLU TYR SER ALA LYS PHE ASP LYS THR THR VAL THR ALA
SEQRES 6 A 434 LEU LYS VAL SER ALA GLU GLU ILE ALA ALA ALA SER GLU
SEQRES 7 A 434 ARG LEU SER ASP GLU LEU LYS GLN ALA MSE ALA VAL ALA
SEQRES 8 A 434 VAL LYS ASN ILE GLU THR PHE HIS THR ALA GLN LYS LEU
SEQRES 9 A 434 PRO PRO VAL ASP VAL GLU THR GLN PRO GLY VAL ARG CYS
SEQRES 10 A 434 GLN GLN VAL THR ARG PRO VAL ALA SER VAL GLY LEU TYR
SEQRES 11 A 434 ILE PRO GLY GLY SER ALA PRO LEU PHE SER THR VAL LEU
SEQRES 12 A 434 MSE LEU ALA THR PRO ALA SER ILE ALA GLY CYS LYS LYS
SEQRES 13 A 434 VAL VAL LEU CYS SER PRO PRO PRO ILE ALA ASP GLU ILE
SEQRES 14 A 434 LEU TYR ALA ALA GLN LEU CYS GLY VAL GLN ASP VAL PHE
SEQRES 15 A 434 ASN VAL GLY GLY ALA GLN ALA ILE ALA ALA LEU ALA PHE
SEQRES 16 A 434 GLY THR GLU SER VAL PRO LYS VAL ASP LYS ILE PHE GLY
SEQRES 17 A 434 PRO GLY ASN ALA PHE VAL THR GLU ALA LYS ARG GLN VAL
SEQRES 18 A 434 SER GLN ARG LEU ASP GLY ALA ALA ILE ASP MSE PRO ALA
SEQRES 19 A 434 GLY PRO SER GLU VAL LEU VAL ILE ALA ASP SER GLY ALA
SEQRES 20 A 434 THR PRO ASP PHE VAL ALA SER ASP LEU LEU SER GLN ALA
SEQRES 21 A 434 GLU HIS GLY PRO ASP SER GLN VAL ILE LEU LEU THR PRO
SEQRES 22 A 434 ALA ALA ASP MSE ALA ARG ARG VAL ALA GLU ALA VAL GLU
SEQRES 23 A 434 ARG GLN LEU ALA GLU LEU PRO ARG ALA GLU THR ALA ARG
SEQRES 24 A 434 GLN ALA LEU ASN ALA SER ARG LEU ILE VAL THR LYS ASP
SEQRES 25 A 434 LEU ALA GLN CYS VAL GLU ILE SER ASN GLN TYR GLY PRO
SEQRES 26 A 434 GLU HIS LEU ILE ILE GLN THR ARG ASN ALA ARG GLU LEU
SEQRES 27 A 434 VAL ASP SER ILE THR SER ALA GLY SER VAL PHE LEU GLY
SEQRES 28 A 434 ASP TRP SER PRO GLU SER ALA GLY ASP TYR ALA SER GLY
SEQRES 29 A 434 THR ASN HIS VAL LEU PRO THR TYR GLY TYR THR ALA THR
SEQRES 30 A 434 CYS SER SER LEU GLY LEU ALA ASP PHE GLN LYS ARG MSE
SEQRES 31 A 434 THR VAL GLN GLU LEU SER LYS GLU GLY PHE SER ALA LEU
SEQRES 32 A 434 ALA SER THR ILE GLU THR LEU ALA ALA ALA GLU ARG LEU
SEQRES 33 A 434 THR ALA HIS LYS ASN ALA VAL THR LEU ARG VAL ASN ALA
SEQRES 34 A 434 LEU LYS GLU GLN ALA
SEQRES 1 B 434 MSE SER PHE ASN THR ILE ILE ASP TRP ASN SER CYS THR
SEQRES 2 B 434 ALA GLU GLN GLN ARG GLN LEU LEU MSE ARG PRO ALA ILE
SEQRES 3 B 434 SER ALA SER GLU SER ILE THR ARG THR VAL ASN ASP ILE
SEQRES 4 B 434 LEU ASP ASN VAL LYS ALA ARG GLY ASP GLU ALA LEU ARG
SEQRES 5 B 434 GLU TYR SER ALA LYS PHE ASP LYS THR THR VAL THR ALA
SEQRES 6 B 434 LEU LYS VAL SER ALA GLU GLU ILE ALA ALA ALA SER GLU
SEQRES 7 B 434 ARG LEU SER ASP GLU LEU LYS GLN ALA MSE ALA VAL ALA
SEQRES 8 B 434 VAL LYS ASN ILE GLU THR PHE HIS THR ALA GLN LYS LEU
SEQRES 9 B 434 PRO PRO VAL ASP VAL GLU THR GLN PRO GLY VAL ARG CYS
SEQRES 10 B 434 GLN GLN VAL THR ARG PRO VAL ALA SER VAL GLY LEU TYR
SEQRES 11 B 434 ILE PRO GLY GLY SER ALA PRO LEU PHE SER THR VAL LEU
SEQRES 12 B 434 MSE LEU ALA THR PRO ALA SER ILE ALA GLY CYS LYS LYS
SEQRES 13 B 434 VAL VAL LEU CYS SER PRO PRO PRO ILE ALA ASP GLU ILE
SEQRES 14 B 434 LEU TYR ALA ALA GLN LEU CYS GLY VAL GLN ASP VAL PHE
SEQRES 15 B 434 ASN VAL GLY GLY ALA GLN ALA ILE ALA ALA LEU ALA PHE
SEQRES 16 B 434 GLY THR GLU SER VAL PRO LYS VAL ASP LYS ILE PHE GLY
SEQRES 17 B 434 PRO GLY ASN ALA PHE VAL THR GLU ALA LYS ARG GLN VAL
SEQRES 18 B 434 SER GLN ARG LEU ASP GLY ALA ALA ILE ASP MSE PRO ALA
SEQRES 19 B 434 GLY PRO SER GLU VAL LEU VAL ILE ALA ASP SER GLY ALA
SEQRES 20 B 434 THR PRO ASP PHE VAL ALA SER ASP LEU LEU SER GLN ALA
SEQRES 21 B 434 GLU HIS GLY PRO ASP SER GLN VAL ILE LEU LEU THR PRO
SEQRES 22 B 434 ALA ALA ASP MSE ALA ARG ARG VAL ALA GLU ALA VAL GLU
SEQRES 23 B 434 ARG GLN LEU ALA GLU LEU PRO ARG ALA GLU THR ALA ARG
SEQRES 24 B 434 GLN ALA LEU ASN ALA SER ARG LEU ILE VAL THR LYS ASP
SEQRES 25 B 434 LEU ALA GLN CYS VAL GLU ILE SER ASN GLN TYR GLY PRO
SEQRES 26 B 434 GLU HIS LEU ILE ILE GLN THR ARG ASN ALA ARG GLU LEU
SEQRES 27 B 434 VAL ASP SER ILE THR SER ALA GLY SER VAL PHE LEU GLY
SEQRES 28 B 434 ASP TRP SER PRO GLU SER ALA GLY ASP TYR ALA SER GLY
SEQRES 29 B 434 THR ASN HIS VAL LEU PRO THR TYR GLY TYR THR ALA THR
SEQRES 30 B 434 CYS SER SER LEU GLY LEU ALA ASP PHE GLN LYS ARG MSE
SEQRES 31 B 434 THR VAL GLN GLU LEU SER LYS GLU GLY PHE SER ALA LEU
SEQRES 32 B 434 ALA SER THR ILE GLU THR LEU ALA ALA ALA GLU ARG LEU
SEQRES 33 B 434 THR ALA HIS LYS ASN ALA VAL THR LEU ARG VAL ASN ALA
SEQRES 34 B 434 LEU LYS GLU GLN ALA
MODRES 1KAH MSE A 22 MET SELENOMETHIONINE
MODRES 1KAH MSE A 88 MET SELENOMETHIONINE
MODRES 1KAH MSE A 144 MET SELENOMETHIONINE
MODRES 1KAH MSE A 232 MET SELENOMETHIONINE
MODRES 1KAH MSE A 277 MET SELENOMETHIONINE
MODRES 1KAH MSE A 390 MET SELENOMETHIONINE
MODRES 1KAH MSE B 1 MET SELENOMETHIONINE
MODRES 1KAH MSE B 22 MET SELENOMETHIONINE
MODRES 1KAH MSE B 88 MET SELENOMETHIONINE
MODRES 1KAH MSE B 144 MET SELENOMETHIONINE
MODRES 1KAH MSE B 232 MET SELENOMETHIONINE
MODRES 1KAH MSE B 277 MET SELENOMETHIONINE
MODRES 1KAH MSE B 390 MET SELENOMETHIONINE
HET MSE A 22 8
HET MSE A 88 8
HET MSE A 144 8
HET MSE A 232 8
HET MSE A 277 8
HET MSE A 390 8
HET MSE B 1 4
HET MSE B 22 8
HET MSE B 88 8
HET MSE B 144 8
HET MSE B 232 8
HET MSE B 277 8
HET MSE B 390 8
HET ZN A 501 1
HET HIS A 502 11
HET HIS A 503 11
HET ZN B 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM HIS HISTIDINE
FORMUL 1 MSE 13(C5 H11 N O2 SE)
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 HIS 2(C6 H10 N3 O2 1+)
HELIX 1 1 ASN A 10 CYS A 12 5 3
HELIX 2 2 THR A 13 MSE A 22 1 10
HELIX 3 3 SER A 29 PHE A 58 1 30
HELIX 4 4 SER A 69 LEU A 80 1 12
HELIX 5 5 SER A 81 ALA A 101 1 21
HELIX 6 6 PHE A 139 GLY A 153 1 15
HELIX 7 7 ALA A 166 CYS A 176 1 11
HELIX 8 8 GLY A 185 GLY A 196 1 12
HELIX 9 9 ASN A 211 GLN A 223 1 13
HELIX 10 10 THR A 248 GLU A 261 1 14
HELIX 11 11 ALA A 274 ALA A 290 1 17
HELIX 12 12 ALA A 295 ASN A 303 1 9
HELIX 13 13 ASP A 312 GLY A 324 1 13
HELIX 14 14 ASN A 334 VAL A 339 1 6
HELIX 15 15 ASP A 340 ILE A 342 5 3
HELIX 16 16 PRO A 355 ALA A 362 1 8
HELIX 17 17 GLY A 373 THR A 377 5 5
HELIX 18 18 GLY A 382 ASP A 385 5 4
HELIX 19 19 SER A 396 GLU A 414 1 19
HELIX 20 20 LEU A 416 ALA A 434 1 19
HELIX 21 21 ASN B 10 CYS B 12 5 3
HELIX 22 22 THR B 13 LEU B 21 1 9
HELIX 23 23 SER B 29 PHE B 58 1 30
HELIX 24 24 SER B 69 LEU B 80 1 12
HELIX 25 25 SER B 81 ALA B 101 1 21
HELIX 26 26 PHE B 139 GLY B 153 1 15
HELIX 27 27 ALA B 166 CYS B 176 1 11
HELIX 28 28 GLY B 185 GLY B 196 1 12
HELIX 29 29 ASN B 211 ARG B 224 1 14
HELIX 30 30 THR B 248 GLU B 261 1 14
HELIX 31 31 ALA B 274 ALA B 290 1 17
HELIX 32 32 ALA B 295 ASN B 303 1 9
HELIX 33 33 ASP B 312 GLY B 324 1 13
HELIX 34 34 ASN B 334 ASP B 340 1 7
HELIX 35 35 PRO B 355 ALA B 362 1 8
HELIX 36 36 GLY B 373 THR B 377 5 5
HELIX 37 37 GLY B 382 ASP B 385 5 4
HELIX 38 38 SER B 396 GLU B 414 1 19
HELIX 39 39 LEU B 416 ALA B 434 1 19
SHEET 1 A 9 ILE A 7 ASP A 8 0
SHEET 2 A 9 ARG A 306 VAL A 309 1 O VAL A 309 N ILE A 7
SHEET 3 A 9 GLN A 267 THR A 272 1 N LEU A 270 O ARG A 306
SHEET 4 A 9 GLU A 238 ALA A 243 1 N VAL A 241 O ILE A 269
SHEET 5 A 9 HIS A 327 GLN A 331 1 O ILE A 329 N ILE A 242
SHEET 6 A 9 SER A 347 LEU A 350 1 O PHE A 349 N ILE A 330
SHEET 7 A 9 GLN B 387 LEU B 395 1 O THR B 391 N VAL A 348
SHEET 8 A 9 VAL B 115 PRO B 123 -1 N GLN B 118 O VAL B 392
SHEET 9 A 9 VAL B 107 GLN B 112 -1 N VAL B 109 O CYS B 117
SHEET 1 B 9 VAL A 107 GLN A 112 0
SHEET 2 B 9 VAL A 115 PRO A 123 -1 O CYS A 117 N VAL A 109
SHEET 3 B 9 GLN A 387 LEU A 395 -1 O VAL A 392 N GLN A 118
SHEET 4 B 9 SER B 347 LEU B 350 1 O VAL B 348 N THR A 391
SHEET 5 B 9 HIS B 327 GLN B 331 1 N ILE B 330 O PHE B 349
SHEET 6 B 9 GLU B 238 ALA B 243 1 N ILE B 242 O ILE B 329
SHEET 7 B 9 GLN B 267 THR B 272 1 O LEU B 271 N VAL B 241
SHEET 8 B 9 ARG B 306 VAL B 309 1 O ILE B 308 N LEU B 270
SHEET 9 B 9 ILE B 7 ASP B 8 1 N ILE B 7 O VAL B 309
SHEET 1 C 5 ASP A 180 ASN A 183 0
SHEET 2 C 5 LYS A 156 SER A 161 1 N LEU A 159 O PHE A 182
SHEET 3 C 5 SER A 126 TYR A 130 1 N LEU A 129 O VAL A 158
SHEET 4 C 5 LYS A 205 PHE A 207 1 O PHE A 207 N GLY A 128
SHEET 5 C 5 ALA A 229 ILE A 230 1 O ALA A 229 N ILE A 206
SHEET 1 D 5 ASP B 180 ASN B 183 0
SHEET 2 D 5 LYS B 156 SER B 161 1 N LEU B 159 O PHE B 182
SHEET 3 D 5 SER B 126 TYR B 130 1 N LEU B 129 O VAL B 158
SHEET 4 D 5 LYS B 205 PHE B 207 1 O PHE B 207 N GLY B 128
SHEET 5 D 5 ALA B 229 ILE B 230 1 O ALA B 229 N ILE B 206
LINK C LEU A 21 N MSE A 22 1555 1555 1.33
LINK C MSE A 22 N ARG A 23 1555 1555 1.33
LINK C ALA A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N ALA A 89 1555 1555 1.33
LINK C LEU A 143 N MSE A 144 1555 1555 1.33
LINK C MSE A 144 N LEU A 145 1555 1555 1.33
LINK C ASP A 231 N MSE A 232 1555 1555 1.33
LINK C MSE A 232 N PRO A 233 1555 1555 1.34
LINK C ASP A 276 N MSE A 277 1555 1555 1.33
LINK C MSE A 277 N ALA A 278 1555 1555 1.33
LINK C ARG A 389 N MSE A 390 1555 1555 1.33
LINK C MSE A 390 N THR A 391 1555 1555 1.33
LINK C MSE B 1 N SER B 2 1555 1555 1.33
LINK C LEU B 21 N MSE B 22 1555 1555 1.33
LINK C MSE B 22 N ARG B 23 1555 1555 1.33
LINK C ALA B 87 N MSE B 88 1555 1555 1.33
LINK C MSE B 88 N ALA B 89 1555 1555 1.33
LINK C LEU B 143 N MSE B 144 1555 1555 1.33
LINK C MSE B 144 N LEU B 145 1555 1555 1.33
LINK C ASP B 231 N MSE B 232 1555 1555 1.33
LINK C MSE B 232 N PRO B 233 1555 1555 1.34
LINK C ASP B 276 N MSE B 277 1555 1555 1.33
LINK C MSE B 277 N ALA B 278 1555 1555 1.33
LINK C ARG B 389 N MSE B 390 1555 1555 1.32
LINK C MSE B 390 N THR B 391 1555 1555 1.33
LINK NE2 HIS A 262 ZN ZN A 501 1555 1555 2.28
LINK OD2 ASP A 360 ZN ZN A 501 1555 1555 2.16
LINK NE2 HIS A 419 ZN ZN B 502 1555 1555 2.08
LINK ZN ZN A 501 N HIS A 502 1555 1555 2.28
LINK ZN ZN A 501 ND1 HIS A 502 1555 1555 1.95
LINK ZN ZN A 501 NE2 HIS B 419 1555 1555 2.20
LINK ND1 HIS A 503 ZN ZN B 502 1555 1555 2.32
LINK NE2 HIS B 262 ZN ZN B 502 1555 1555 2.02
LINK OD2 ASP B 360 ZN ZN B 502 1555 1555 1.87
CISPEP 1 PRO A 163 PRO A 164 0 0.19
CISPEP 2 PRO B 163 PRO B 164 0 -0.37
SITE 1 AC1 5 HIS A 262 GLU A 356 ASP A 360 HIS A 502
SITE 2 AC1 5 HIS B 419
SITE 1 AC2 5 HIS A 419 HIS A 503 HIS B 262 GLU B 356
SITE 2 AC2 5 ASP B 360
SITE 1 AC3 13 LEU A 138 SER A 237 HIS A 262 GLU A 326
SITE 2 AC3 13 HIS A 327 GLU A 356 ASP A 360 TYR A 361
SITE 3 AC3 13 HIS A 367 ZN A 501 GLU B 414 LEU B 416
SITE 4 AC3 13 HIS B 419
SITE 1 AC4 9 GLU A 414 LEU A 416 HIS A 419 SER B 140
SITE 2 AC4 9 HIS B 262 ASP B 360 TYR B 361 HIS B 367
SITE 3 AC4 9 ZN B 502
CRYST1 55.260 109.090 157.940 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018096 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009167 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
