HEADER OXIDOREDUCTASE 10-FEB-06 2FZW
TITLE STRUCTURE OF THE BINARY COMPLEX OF THE E67L MUTANT OF HUMAN
TITLE 2 GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE WITH NAD(H)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE CLASS III CHI CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE;
COMPND 5 SYNONYM: S- HYDROXYMETHYL, GLUTATHIONE DEHYDROGENASE, GLUTATHIONE-
COMPND 6 DEPENDENT FORMALDEHYDE DEHYDROGENASE, FDH;
COMPND 7 EC: 1.1.1.1, 1.1.1.284;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADH5, ADHX, FDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS S-NITROSOGLUTATHIONE REDUCTASE, GLUTATHIONE-DEPENDENT FORMALDEHYDE
KEYWDS 2 DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.SANGHANI,H.ROBINSON
REVDAT 5 14-FEB-24 2FZW 1 REMARK
REVDAT 4 20-OCT-21 2FZW 1 REMARK SEQADV LINK
REVDAT 3 18-OCT-17 2FZW 1 REMARK
REVDAT 2 24-FEB-09 2FZW 1 VERSN
REVDAT 1 13-JUN-06 2FZW 0
JRNL AUTH P.C.SANGHANI,W.I.DAVIS,L.ZHAI,H.ROBINSON
JRNL TITL STRUCTURE-FUNCTION RELATIONSHIPS IN HUMAN
JRNL TITL 2 GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE. ROLE OF
JRNL TITL 3 GLU-67 AND ARG-368 IN THE CATALYTIC MECHANISM.
JRNL REF BIOCHEMISTRY V. 45 4819 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16605250
JRNL DOI 10.1021/BI052554Q
REMARK 2
REMARK 2 RESOLUTION. 1.84 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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 87208
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4402
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1477
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 77
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5542
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 109
REMARK 3 SOLVENT ATOMS : 1021
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.21600
REMARK 3 B22 (A**2) : -3.21600
REMARK 3 B33 (A**2) : 6.43200
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) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.08
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 46.47
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_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NADH.PAR
REMARK 3 PARAMETER FILE 5 : 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 : NADH.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87310
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 28.30
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 26.20
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 8000, 100MM POTASSIUM
REMARK 280 PHOSPHATE, PH 7.1, 10UM ZINC SULFATE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 155.84000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.63500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.63500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 233.76000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.63500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.63500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.92000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.63500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.63500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 233.76000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.63500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.63500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.92000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 155.84000
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: 7020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 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 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 PHE A 145 47.63 -83.60
REMARK 500 LYS A 167 -52.77 -121.87
REMARK 500 CYS A 173 -94.42 -155.77
REMARK 500 CYS A 173 -87.45 -161.88
REMARK 500 VAL A 341 -50.54 -142.20
REMARK 500 ILE A 367 -61.27 -108.89
REMARK 500 GLN B 95 89.99 -150.03
REMARK 500 PHE B 145 47.94 -84.84
REMARK 500 LYS B 167 -54.06 -122.81
REMARK 500 CYS B 173 -93.08 -156.02
REMARK 500 TRP B 285 -0.27 -143.80
REMARK 500 VAL B 341 -48.23 -140.30
REMARK 500 ILE B 367 -64.16 -108.11
REMARK 500
REMARK 500 REMARK: NULL
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 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 44 SG
REMARK 620 2 HIS A 66 NE2 101.6
REMARK 620 3 CYS A 173 SG 129.8 120.9
REMARK 620 4 HOH A1805 O 101.0 103.0 94.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 99 SG 109.1
REMARK 620 3 CYS A 102 SG 117.1 106.1
REMARK 620 4 CYS A 110 SG 104.7 118.0 102.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1804 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 186 O
REMARK 620 2 LYS A 187 O 67.5
REMARK 620 3 GLU A 189 OE2 141.0 87.0
REMARK 620 4 TYR A 263 OH 85.9 93.2 65.9
REMARK 620 5 HOH B2859 O 89.6 156.5 109.9 79.7
REMARK 620 6 HOH B2860 O 82.0 108.9 135.6 148.1 70.8
REMARK 620 7 HOH B2875 O 148.1 143.8 65.2 95.7 59.7 80.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 376 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 44 SG
REMARK 620 2 HIS B 66 NE2 105.9
REMARK 620 3 CYS B 173 SG 125.9 117.4
REMARK 620 4 HOH B2463 O 102.8 107.0 94.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 375 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 96 SG
REMARK 620 2 CYS B 99 SG 110.9
REMARK 620 3 CYS B 102 SG 114.0 105.1
REMARK 620 4 CYS B 110 SG 105.8 117.8 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1805 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 186 O
REMARK 620 2 LYS B 187 O 67.8
REMARK 620 3 GLU B 189 OE2 140.4 84.8
REMARK 620 4 TYR B 263 OH 87.0 91.5 64.9
REMARK 620 5 HOH B2732 O 90.1 157.3 111.4 81.8
REMARK 620 6 HOH B2741 O 145.1 143.2 72.0 103.3 59.4
REMARK 620 7 HOH B2898 O 78.6 108.0 139.0 148.8 70.8 75.6
REMARK 620 8 HOH B2917 O 130.6 73.4 60.2 123.9 128.1 70.4 85.7
REMARK 620 N 1 2 3 4 5 6 7
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 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 1377
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 2377
DBREF 2FZW A 1 373 UNP P11766 ADHX_HUMAN 1 373
DBREF 2FZW B 1 373 UNP P11766 ADHX_HUMAN 1 373
SEQADV 2FZW LEU A 67 UNP P11766 GLU 67 ENGINEERED MUTATION
SEQADV 2FZW LEU B 67 UNP P11766 GLU 67 ENGINEERED MUTATION
SEQRES 1 A 373 ALA ASN GLU VAL ILE LYS CYS LYS ALA ALA VAL ALA TRP
SEQRES 2 A 373 GLU ALA GLY LYS PRO LEU SER ILE GLU GLU ILE GLU VAL
SEQRES 3 A 373 ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS ILE ILE
SEQRES 4 A 373 ALA THR ALA VAL CYS HIS THR ASP ALA TYR THR LEU SER
SEQRES 5 A 373 GLY ALA ASP PRO GLU GLY CYS PHE PRO VAL ILE LEU GLY
SEQRES 6 A 373 HIS LEU GLY ALA GLY ILE VAL GLU SER VAL GLY GLU GLY
SEQRES 7 A 373 VAL THR LYS LEU LYS ALA GLY ASP THR VAL ILE PRO LEU
SEQRES 8 A 373 TYR ILE PRO GLN CYS GLY GLU CYS LYS PHE CYS LEU ASN
SEQRES 9 A 373 PRO LYS THR ASN LEU CYS GLN LYS ILE ARG VAL THR GLN
SEQRES 10 A 373 GLY LYS GLY LEU MET PRO ASP GLY THR SER ARG PHE THR
SEQRES 11 A 373 CYS LYS GLY LYS THR ILE LEU HIS TYR MET GLY THR SER
SEQRES 12 A 373 THR PHE SER GLU TYR THR VAL VAL ALA ASP ILE SER VAL
SEQRES 13 A 373 ALA LYS ILE ASP PRO LEU ALA PRO LEU ASP LYS VAL CYS
SEQRES 14 A 373 LEU LEU GLY CYS GLY ILE SER THR GLY TYR GLY ALA ALA
SEQRES 15 A 373 VAL ASN THR ALA LYS LEU GLU PRO GLY SER VAL CYS ALA
SEQRES 16 A 373 VAL PHE GLY LEU GLY GLY VAL GLY LEU ALA VAL ILE MET
SEQRES 17 A 373 GLY CYS LYS VAL ALA GLY ALA SER ARG ILE ILE GLY VAL
SEQRES 18 A 373 ASP ILE ASN LYS ASP LYS PHE ALA ARG ALA LYS GLU PHE
SEQRES 19 A 373 GLY ALA THR GLU CYS ILE ASN PRO GLN ASP PHE SER LYS
SEQRES 20 A 373 PRO ILE GLN GLU VAL LEU ILE GLU MET THR ASP GLY GLY
SEQRES 21 A 373 VAL ASP TYR SER PHE GLU CYS ILE GLY ASN VAL LYS VAL
SEQRES 22 A 373 MET ARG ALA ALA LEU GLU ALA CYS HIS LYS GLY TRP GLY
SEQRES 23 A 373 VAL SER VAL VAL VAL GLY VAL ALA ALA SER GLY GLU GLU
SEQRES 24 A 373 ILE ALA THR ARG PRO PHE GLN LEU VAL THR GLY ARG THR
SEQRES 25 A 373 TRP LYS GLY THR ALA PHE GLY GLY TRP LYS SER VAL GLU
SEQRES 26 A 373 SER VAL PRO LYS LEU VAL SER GLU TYR MET SER LYS LYS
SEQRES 27 A 373 ILE LYS VAL ASP GLU PHE VAL THR HIS ASN LEU SER PHE
SEQRES 28 A 373 ASP GLU ILE ASN LYS ALA PHE GLU LEU MET HIS SER GLY
SEQRES 29 A 373 LYS SER ILE ARG THR VAL VAL LYS ILE
SEQRES 1 B 373 ALA ASN GLU VAL ILE LYS CYS LYS ALA ALA VAL ALA TRP
SEQRES 2 B 373 GLU ALA GLY LYS PRO LEU SER ILE GLU GLU ILE GLU VAL
SEQRES 3 B 373 ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS ILE ILE
SEQRES 4 B 373 ALA THR ALA VAL CYS HIS THR ASP ALA TYR THR LEU SER
SEQRES 5 B 373 GLY ALA ASP PRO GLU GLY CYS PHE PRO VAL ILE LEU GLY
SEQRES 6 B 373 HIS LEU GLY ALA GLY ILE VAL GLU SER VAL GLY GLU GLY
SEQRES 7 B 373 VAL THR LYS LEU LYS ALA GLY ASP THR VAL ILE PRO LEU
SEQRES 8 B 373 TYR ILE PRO GLN CYS GLY GLU CYS LYS PHE CYS LEU ASN
SEQRES 9 B 373 PRO LYS THR ASN LEU CYS GLN LYS ILE ARG VAL THR GLN
SEQRES 10 B 373 GLY LYS GLY LEU MET PRO ASP GLY THR SER ARG PHE THR
SEQRES 11 B 373 CYS LYS GLY LYS THR ILE LEU HIS TYR MET GLY THR SER
SEQRES 12 B 373 THR PHE SER GLU TYR THR VAL VAL ALA ASP ILE SER VAL
SEQRES 13 B 373 ALA LYS ILE ASP PRO LEU ALA PRO LEU ASP LYS VAL CYS
SEQRES 14 B 373 LEU LEU GLY CYS GLY ILE SER THR GLY TYR GLY ALA ALA
SEQRES 15 B 373 VAL ASN THR ALA LYS LEU GLU PRO GLY SER VAL CYS ALA
SEQRES 16 B 373 VAL PHE GLY LEU GLY GLY VAL GLY LEU ALA VAL ILE MET
SEQRES 17 B 373 GLY CYS LYS VAL ALA GLY ALA SER ARG ILE ILE GLY VAL
SEQRES 18 B 373 ASP ILE ASN LYS ASP LYS PHE ALA ARG ALA LYS GLU PHE
SEQRES 19 B 373 GLY ALA THR GLU CYS ILE ASN PRO GLN ASP PHE SER LYS
SEQRES 20 B 373 PRO ILE GLN GLU VAL LEU ILE GLU MET THR ASP GLY GLY
SEQRES 21 B 373 VAL ASP TYR SER PHE GLU CYS ILE GLY ASN VAL LYS VAL
SEQRES 22 B 373 MET ARG ALA ALA LEU GLU ALA CYS HIS LYS GLY TRP GLY
SEQRES 23 B 373 VAL SER VAL VAL VAL GLY VAL ALA ALA SER GLY GLU GLU
SEQRES 24 B 373 ILE ALA THR ARG PRO PHE GLN LEU VAL THR GLY ARG THR
SEQRES 25 B 373 TRP LYS GLY THR ALA PHE GLY GLY TRP LYS SER VAL GLU
SEQRES 26 B 373 SER VAL PRO LYS LEU VAL SER GLU TYR MET SER LYS LYS
SEQRES 27 B 373 ILE LYS VAL ASP GLU PHE VAL THR HIS ASN LEU SER PHE
SEQRES 28 B 373 ASP GLU ILE ASN LYS ALA PHE GLU LEU MET HIS SER GLY
SEQRES 29 B 373 LYS SER ILE ARG THR VAL VAL LYS ILE
HET ZN A 375 1
HET ZN A 376 1
HET PO4 A1803 5
HET K A1804 1
HET NAD A1377 44
HET ZN B 375 1
HET ZN B 376 1
HET PO4 B1801 5
HET PO4 B1802 5
HET K B1805 1
HET NAD B2377 44
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM K POTASSIUM ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 PO4 3(O4 P 3-)
FORMUL 6 K 2(K 1+)
FORMUL 7 NAD 2(C21 H27 N7 O14 P2)
FORMUL 14 HOH *1021(H2 O)
HELIX 1 1 CYS A 44 SER A 52 1 9
HELIX 2 2 CYS A 99 ASN A 104 1 6
HELIX 3 3 ILE A 113 LYS A 119 1 7
HELIX 4 4 PRO A 164 CYS A 169 1 6
HELIX 5 5 LEU A 170 GLY A 172 5 3
HELIX 6 6 CYS A 173 ASN A 184 1 12
HELIX 7 7 GLY A 200 GLY A 214 1 15
HELIX 8 8 ASN A 224 ASP A 226 5 3
HELIX 9 9 LYS A 227 GLY A 235 1 9
HELIX 10 10 ASN A 241 PHE A 245 5 5
HELIX 11 11 PRO A 248 THR A 257 1 10
HELIX 12 12 ASN A 270 ALA A 280 1 11
HELIX 13 13 PRO A 304 THR A 309 1 6
HELIX 14 14 ALA A 317 TRP A 321 5 5
HELIX 15 15 LYS A 322 SER A 336 1 15
HELIX 16 16 VAL A 341 GLU A 343 5 3
HELIX 17 17 GLU A 353 SER A 363 1 11
HELIX 18 18 CYS B 44 SER B 52 1 9
HELIX 19 19 CYS B 99 ASN B 104 1 6
HELIX 20 20 ILE B 113 LYS B 119 1 7
HELIX 21 21 PRO B 164 CYS B 169 1 6
HELIX 22 22 LEU B 170 GLY B 172 5 3
HELIX 23 23 CYS B 173 ASN B 184 1 12
HELIX 24 24 GLY B 200 ALA B 213 1 14
HELIX 25 25 ASN B 224 ASP B 226 5 3
HELIX 26 26 LYS B 227 GLY B 235 1 9
HELIX 27 27 ASN B 241 PHE B 245 5 5
HELIX 28 28 PRO B 248 THR B 257 1 10
HELIX 29 29 ASN B 270 ALA B 280 1 11
HELIX 30 30 PRO B 304 THR B 309 1 6
HELIX 31 31 LYS B 322 SER B 336 1 15
HELIX 32 32 VAL B 341 GLU B 343 5 3
HELIX 33 33 GLU B 353 GLY B 364 1 12
SHEET 1 A 4 ILE A 5 VAL A 11 0
SHEET 2 A 4 SER A 20 VAL A 26 -1 O ILE A 24 N CYS A 7
SHEET 3 A 4 PHE A 129 CYS A 131 -1 O THR A 130 N GLU A 25
SHEET 4 A 4 LYS A 134 ILE A 136 -1 O LYS A 134 N CYS A 131
SHEET 1 B 5 TYR A 148 ALA A 152 0
SHEET 2 B 5 GLU A 33 ALA A 42 -1 N VAL A 34 O VAL A 151
SHEET 3 B 5 LEU A 67 VAL A 75 -1 O ILE A 71 N LYS A 37
SHEET 4 B 5 THR A 87 PRO A 90 -1 O VAL A 88 N GLY A 70
SHEET 5 B 5 VAL A 156 LYS A 158 -1 O ALA A 157 N ILE A 89
SHEET 1 C 4 TYR A 148 ALA A 152 0
SHEET 2 C 4 GLU A 33 ALA A 42 -1 N VAL A 34 O VAL A 151
SHEET 3 C 4 ARG A 368 LYS A 372 -1 O VAL A 371 N THR A 41
SHEET 4 C 4 VAL A 345 SER A 350 1 N LEU A 349 O LYS A 372
SHEET 1 D 6 GLU A 238 ILE A 240 0
SHEET 2 D 6 ARG A 217 VAL A 221 1 N GLY A 220 O ILE A 240
SHEET 3 D 6 VAL A 193 PHE A 197 1 N CYS A 194 O ARG A 217
SHEET 4 D 6 TYR A 263 GLU A 266 1 O PHE A 265 N PHE A 197
SHEET 5 D 6 VAL A 287 VAL A 290 1 O VAL A 289 N SER A 264
SHEET 6 D 6 THR A 312 GLY A 315 1 O LYS A 314 N SER A 288
SHEET 1 E 2 ILE A 300 THR A 302 0
SHEET 2 E 2 ILE B 300 THR B 302 -1 O ILE B 300 N THR A 302
SHEET 1 F 4 ILE B 5 VAL B 11 0
SHEET 2 F 4 SER B 20 VAL B 26 -1 O ILE B 24 N CYS B 7
SHEET 3 F 4 PHE B 129 CYS B 131 -1 O THR B 130 N GLU B 25
SHEET 4 F 4 LYS B 134 ILE B 136 -1 O LYS B 134 N CYS B 131
SHEET 1 G 5 TYR B 148 ALA B 152 0
SHEET 2 G 5 GLU B 33 ALA B 42 -1 N ILE B 36 O THR B 149
SHEET 3 G 5 LEU B 67 VAL B 75 -1 O ILE B 71 N LYS B 37
SHEET 4 G 5 THR B 87 PRO B 90 -1 O VAL B 88 N GLY B 70
SHEET 5 G 5 VAL B 156 LYS B 158 -1 O ALA B 157 N ILE B 89
SHEET 1 H 4 TYR B 148 ALA B 152 0
SHEET 2 H 4 GLU B 33 ALA B 42 -1 N ILE B 36 O THR B 149
SHEET 3 H 4 ARG B 368 LYS B 372 -1 O VAL B 371 N THR B 41
SHEET 4 H 4 VAL B 345 SER B 350 1 N LEU B 349 O LYS B 372
SHEET 1 I 6 GLU B 238 ILE B 240 0
SHEET 2 I 6 ARG B 217 VAL B 221 1 N GLY B 220 O GLU B 238
SHEET 3 I 6 VAL B 193 PHE B 197 1 N CYS B 194 O ILE B 219
SHEET 4 I 6 TYR B 263 GLU B 266 1 O PHE B 265 N PHE B 197
SHEET 5 I 6 VAL B 287 VAL B 291 1 O VAL B 289 N SER B 264
SHEET 6 I 6 THR B 312 THR B 316 1 O LYS B 314 N SER B 288
LINK SG CYS A 44 ZN ZN A 376 1555 1555 2.49
LINK NE2 HIS A 66 ZN ZN A 376 1555 1555 2.19
LINK SG CYS A 96 ZN ZN A 375 1555 1555 2.39
LINK SG CYS A 99 ZN ZN A 375 1555 1555 2.39
LINK SG CYS A 102 ZN ZN A 375 1555 1555 2.39
LINK SG CYS A 110 ZN ZN A 375 1555 1555 2.38
LINK SG ACYS A 173 ZN ZN A 376 1555 1555 2.38
LINK O ALA A 186 K K A1804 1555 1555 2.97
LINK O LYS A 187 K K A1804 1555 1555 3.05
LINK OE2 GLU A 189 K K A1804 1555 1555 3.15
LINK OH TYR A 263 K K A1804 1555 1555 2.95
LINK ZN ZN A 376 O HOH A1805 1555 1555 2.28
LINK K K A1804 O HOH B2859 1555 1555 3.21
LINK K K A1804 O HOH B2860 1555 1555 3.31
LINK K K A1804 O HOH B2875 1555 1555 3.39
LINK SG CYS B 44 ZN ZN B 376 1555 1555 2.42
LINK NE2 HIS B 66 ZN ZN B 376 1555 1555 2.10
LINK SG CYS B 96 ZN ZN B 375 1555 1555 2.38
LINK SG CYS B 99 ZN ZN B 375 1555 1555 2.39
LINK SG CYS B 102 ZN ZN B 375 1555 1555 2.37
LINK SG CYS B 110 ZN ZN B 375 1555 1555 2.38
LINK SG CYS B 173 ZN ZN B 376 1555 1555 2.37
LINK O ALA B 186 K K B1805 1555 1555 2.95
LINK O LYS B 187 K K B1805 1555 1555 3.04
LINK OE2 GLU B 189 K K B1805 1555 1555 3.15
LINK OH TYR B 263 K K B1805 1555 1555 2.94
LINK ZN ZN B 376 O HOH B2463 1555 1555 2.22
LINK K K B1805 O HOH B2732 1555 1555 3.18
LINK K K B1805 O HOH B2741 1555 1555 3.33
LINK K K B1805 O HOH B2898 1555 1555 3.23
LINK K K B1805 O HOH B2917 1555 1555 3.43
CISPEP 1 PHE A 60 PRO A 61 0 -0.10
CISPEP 2 PHE B 60 PRO B 61 0 -0.15
SITE 1 AC1 4 CYS A 96 CYS A 99 CYS A 102 CYS A 110
SITE 1 AC2 4 CYS A 44 HIS A 66 CYS A 173 HOH A1805
SITE 1 AC3 4 CYS B 96 CYS B 99 CYS B 102 CYS B 110
SITE 1 AC4 4 CYS B 44 HIS B 66 CYS B 173 HOH B2463
SITE 1 AC5 6 LYS A 314 LYS B 314 HOH B2719 HOH B2861
SITE 2 AC5 6 HOH B2892 HOH B2898
SITE 1 AC6 7 PO4 A1803 HOH A2021 LYS B 83 ASP B 86
SITE 2 AC6 7 LYS B 158 HOH B2696 HOH B2855
SITE 1 AC7 7 LYS A 83 LYS A 158 HOH A2068 HOH A2139
SITE 2 AC7 7 LYS B 83 PO4 B1802 HOH B2519
SITE 1 AC8 4 ALA A 186 LYS A 187 GLU A 189 TYR A 263
SITE 1 AC9 4 ALA B 186 LYS B 187 GLU B 189 TYR B 263
SITE 1 BC1 27 HIS A 45 CYS A 173 THR A 177 GLY A 198
SITE 2 BC1 27 GLY A 200 GLY A 201 VAL A 202 ASP A 222
SITE 3 BC1 27 ILE A 223 CYS A 267 ILE A 268 VAL A 291
SITE 4 BC1 27 GLY A 292 VAL A 293 THR A 316 ALA A 317
SITE 5 BC1 27 PHE A 318 ARG A 368 HOH A1817 HOH A1871
SITE 6 BC1 27 HOH A1877 HOH A1901 HOH A1941 HOH A1964
SITE 7 BC1 27 HOH A1987 HOH A1995 HOH A2187
SITE 1 BC2 34 HIS B 45 TYR B 49 GLY B 198 GLY B 200
SITE 2 BC2 34 GLY B 201 VAL B 202 ASP B 222 ILE B 223
SITE 3 BC2 34 CYS B 267 ILE B 268 VAL B 291 GLY B 292
SITE 4 BC2 34 VAL B 293 ARG B 368 HOH B2410 HOH B2453
SITE 5 BC2 34 HOH B2460 HOH B2465 HOH B2502 HOH B2530
SITE 6 BC2 34 HOH B2547 HOH B2564 HOH B2580 HOH B2701
SITE 7 BC2 34 HOH B2739 HOH B2789 HOH B2819 HOH B2853
SITE 8 BC2 34 HOH B2862 HOH B2864 HOH B2876 HOH B2880
SITE 9 BC2 34 HOH B2889 HOH B2916
CRYST1 79.270 79.270 311.680 90.00 90.00 90.00 P 43 21 2 16
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 0.012615 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012615 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003208 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
