HEADER HYDROLASE 10-MAR-08 3CHP
TITLE CRYSTAL STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (3S)-3-
TITLE 2 AMINO-4-OXO-4-[(4-PHENYLMETHOXYPHENYL)AMINO]BUTANOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A(4) HYDROLASE;
COMPND 5 EC: 3.3.2.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LTA4H, LTA4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT3-MB4
KEYWDS EPOXIDE HYDROLASE, ALPHA-BETA PROTEIN, LEUKOTRIENE BIOSYNTHESIS,
KEYWDS 2 METALLOPROTEASE, INHIBITOR COMPLEX, ALTERNATIVE SPLICING, CYTOPLASM,
KEYWDS 3 METAL-BINDING, MULTIFUNCTIONAL ENZYME, ZINC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.G.M.THUNNISSEN,M.ADLER,M.WHITLOW
REVDAT 4 07-MAR-18 3CHP 1 REMARK
REVDAT 3 24-FEB-09 3CHP 1 VERSN
REVDAT 2 27-MAY-08 3CHP 1 JRNL
REVDAT 1 22-APR-08 3CHP 0
JRNL AUTH T.A.KIRKLAND,M.ADLER,J.G.BAUMAN,M.CHEN,J.Z.HAEGGSTROM,
JRNL AUTH 2 B.KING,M.J.KOCHANNY,A.M.LIANG,L.MENDOZA,G.B.PHILLIPS,
JRNL AUTH 3 M.THUNNISSEN,L.TRINH,M.WHITLOW,B.YE,H.YE,J.PARKINSON,
JRNL AUTH 4 W.J.GUILFORD
JRNL TITL SYNTHESIS OF GLUTAMIC ACID ANALOGS AS POTENT INHIBITORS OF
JRNL TITL 2 LEUKOTRIENE A4 HYDROLASE.
JRNL REF BIOORG.MED.CHEM. V. 16 4963 2008
JRNL REFN ISSN 0968-0896
JRNL PMID 18394906
JRNL DOI 10.1016/J.BMC.2008.03.042
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.G.M.THUNNISSEN,P.N.NORDLUND,J.Z.HAEGGSTROM
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE, A
REMARK 1 TITL 2 BIFUNCTIONAL ENZYME IN INFLAMMATION
REMARK 1 REF NAT.STRUCT.BIOL. V. 8 131 2001
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.M.G.M.THUNNISSEN,B.ANDERSON,B.SAMUELSSON,C.-H.WONG,
REMARK 1 AUTH 2 J.Z.HAEGGSTROM
REMARK 1 TITL CRYSTAL STRUCTURES OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX
REMARK 1 TITL 2 WITH CAPTOPRIL AND TWO COMPETITIVE TIGHT-BINDING INHIBITORS.
REMARK 1 REF FASEB J. V. 16 1648 2002
REMARK 1 REFN ISSN 0892-6638
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,B.SAMUELSSON,
REMARK 1 AUTH 2 J.Z.HAEGGSTROM
REMARK 1 TITL LEUKOTRIENE A4 HYDROLASE: SELECTIVE ABROGATION OF
REMARK 1 TITL 2 LEUKOTRIENE B4 FORMATION BY MUTATION OF ASPARTIC ACID 375.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 99 4215 2002
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.C.RUDBERG,F.O.T.THOLANDER,M.ANDBERG,M.M.G.M.THUNNISSEN,
REMARK 1 AUTH 2 J.Z.HAEGGSTROM
REMARK 1 TITL LEUKOTRIENE A4 HYDROLASE: IDENTIFICATION OF A COMMON
REMARK 1 TITL 2 CARBOXYLATE RECOGNITION SITE FOR THE EPOXIDE HYDROLASE AND
REMARK 1 TITL 3 AMINOPEPTIDASE SUBSTRATES
REMARK 1 REF J.MOL.BIOL. V. 279 27376 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2018787.390
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 44475
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 + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2248
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
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) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4104
REMARK 3 BIN R VALUE (WORKING SET) : 0.2659
REMARK 3 BIN FREE R VALUE : 0.2899
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 209
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4861
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.99000
REMARK 3 B22 (A**2) : 3.16000
REMARK 3 B33 (A**2) : -4.15000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.650
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) : 1.780 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.560 ; 2.050
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.670 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.570 ; 3.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 52.36
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 : ZN.PAR
REMARK 3 PARAMETER FILE 5 : 346.PAR
REMARK 3 PARAMETER FILE 6 : IMD.PAR
REMARK 3 PARAMETER FILE 7 : ACE.PAR
REMARK 3 PARAMETER FILE 8 : 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 : ZN.TOP
REMARK 3 TOPOLOGY FILE 5 : 346.TOP
REMARK 3 TOPOLOGY FILE 6 : IMD.TOP
REMARK 3 TOPOLOGY FILE 7 : ACE.TOP
REMARK 3 TOPOLOGY FILE 8 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THERE IS POSITIVE FO-FC DENSITY BETWEEN
REMARK 3 THE ZN ION AND THE CARBOXYL OF THE INHIBITOR, AND AT THE 3
REMARK 3 POSITION OF THE PHENYL-METHYL AT THE OTHER END OF THE INHIBITOR.
REMARK 4
REMARK 4 3CHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046788.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.007
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45016
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 26.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
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) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, IMIDEAZOLE
REMARK 280 PH 6.8, YBCL2, BESTATIN, LIQUID DIFFUSION, TEMPERATURE 298K, PH
REMARK 280 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 33.88350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.78600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.88350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.78600
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1406 LIES ON A SPECIAL POSITION.
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 PRO A 1
REMARK 465 GLU A 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1138 O HOH A 1138 2665 1.16
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A 63 149.73 -176.52
REMARK 500 GLN A 79 65.08 -113.40
REMARK 500 SER A 80 -119.62 45.02
REMARK 500 LYS A 96 126.05 -34.07
REMARK 500 LYS A 126 1.60 -63.81
REMARK 500 PRO A 129 -169.59 -73.72
REMARK 500 ILE A 138 52.12 -118.89
REMARK 500 SER A 185 41.95 -88.55
REMARK 500 GLU A 236 1.13 -67.17
REMARK 500 GLU A 271 44.08 -73.84
REMARK 500 CYS A 274 -23.27 80.51
REMARK 500 LEU A 275 89.31 -150.87
REMARK 500 ASP A 286 12.80 -146.96
REMARK 500 PHE A 432 44.06 -101.01
REMARK 500 PRO A 458 172.09 -57.91
REMARK 500 LYS A 546 34.22 71.45
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 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 295 NE2
REMARK 620 2 HIS A 299 NE2 100.1
REMARK 620 3 GLU A 318 OE1 100.4 112.0
REMARK 620 N 1 2
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 820
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 850
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4BO A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HS6 RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN
REMARK 900 RELATED ID: 1GW6 RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT
REMARK 900 RELATED ID: 1H19 RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE E271Q MUTANT
REMARK 900 RELATED ID: 1SQM RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE R563A MUTANT
REMARK 900 RELATED ID: 3CHO RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 2-AMINO-N-[4-
REMARK 900 (PHENYLMETHOXY)PHENYL]-ACETAMIDE
REMARK 900 RELATED ID: 3CHQ RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH N5-[4-
REMARK 900 (PHENYLMETHOXY)PHENYL]-L-GLUTAMINE
REMARK 900 RELATED ID: 3CHR RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 4-AMINO-N-[4-
REMARK 900 (PHENYLMETHOXY)PHENYL]-BUTANAMIDE
REMARK 900 RELATED ID: 3CHS RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (2S)-2-AMINO-
REMARK 900 5-[[4-[(2S)-2-HYDROXY-2-PHENYL-ETHOXY]PHENYL]AMINO]-5-OXO-PENTANOIC
REMARK 900 ACID
REMARK 900 RELATED ID: 2VJ8 RELATED DB: PDB
REMARK 900 STRUCTURE OF LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH HYDROXAMIC
REMARK 900 ACID BASED INHIBITOR
DBREF 3CHP A 1 610 UNP P09960 LKHA4_HUMAN 2 611
SEQRES 1 A 610 PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO ALA
SEQRES 2 A 610 SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS SER
SEQRES 3 A 610 VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA ALA
SEQRES 4 A 610 LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER LEU
SEQRES 5 A 610 VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL VAL
SEQRES 6 A 610 ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU ARG
SEQRES 7 A 610 GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU PRO
SEQRES 8 A 610 ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU ILE
SEQRES 9 A 610 SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN TRP
SEQRES 10 A 610 LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO TYR
SEQRES 11 A 610 LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA ILE
SEQRES 12 A 610 LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR TYR
SEQRES 13 A 610 THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA LEU
SEQRES 14 A 610 MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO GLU
SEQRES 15 A 610 ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS VAL
SEQRES 16 A 610 PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY ALA
SEQRES 17 A 610 LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL TRP
SEQRES 18 A 610 SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU PHE
SEQRES 19 A 610 SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP LEU
SEQRES 20 A 610 GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU VAL
SEQRES 21 A 610 LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN PRO
SEQRES 22 A 610 CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY ASP
SEQRES 23 A 610 LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER HIS
SEQRES 24 A 610 SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP ASP
SEQRES 25 A 610 HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU GLU
SEQRES 26 A 610 ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE ARG
SEQRES 27 A 610 HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN ASN
SEQRES 28 A 610 SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR LYS
SEQRES 29 A 610 LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL ALA
SEQRES 30 A 610 TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU LEU
SEQRES 31 A 610 PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE PHE
SEQRES 32 A 610 LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER TYR
SEQRES 33 A 610 LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU TYR
SEQRES 34 A 610 SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN VAL
SEQRES 35 A 610 ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO PRO
SEQRES 36 A 610 ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA CYS
SEQRES 37 A 610 ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU ASP
SEQRES 38 A 610 ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP LEU
SEQRES 39 A 610 SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR LEU
SEQRES 40 A 610 GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG MET
SEQRES 41 A 610 GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER GLU
SEQRES 42 A 610 ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER LYS
SEQRES 43 A 610 TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA THR
SEQRES 44 A 610 GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE LYS
SEQRES 45 A 610 ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA VAL
SEQRES 46 A 610 ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO VAL
SEQRES 47 A 610 THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP
HET ZN A 701 1
HET YB A 801 1
HET ACT A 820 4
HET IMD A 850 5
HET 4BO A 901 23
HETNAM ZN ZINC ION
HETNAM YB YTTERBIUM (III) ION
HETNAM ACT ACETATE ION
HETNAM IMD IMIDAZOLE
HETNAM 4BO (3S)-3-AMINO-4-OXO-4-[(4-PHENYLMETHOXYPHENYL)
HETNAM 2 4BO AMINO]BUTANOIC ACID
FORMUL 2 ZN ZN 2+
FORMUL 3 YB YB 3+
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 IMD C3 H5 N2 1+
FORMUL 6 4BO C17 H18 N2 O4
FORMUL 7 HOH *236(H2 O)
HELIX 1 1 GLN A 79 GLY A 83 5 5
HELIX 2 2 THR A 119 THR A 123 5 5
HELIX 3 3 HIS A 139 ILE A 143 5 5
HELIX 4 4 PRO A 198 ILE A 202 5 5
HELIX 5 5 GLU A 223 PHE A 234 1 12
HELIX 6 6 GLU A 236 GLY A 249 1 14
HELIX 7 7 PRO A 280 LEU A 283 5 4
HELIX 8 8 SER A 290 HIS A 299 1 10
HELIX 9 9 THR A 310 ASP A 312 5 3
HELIX 10 10 HIS A 313 GLY A 334 1 22
HELIX 11 11 GLY A 334 GLY A 357 1 24
HELIX 12 12 HIS A 360 LYS A 364 5 5
HELIX 13 13 ASP A 373 TYR A 378 1 6
HELIX 14 14 SER A 380 LEU A 397 1 18
HELIX 15 15 GLY A 399 SER A 415 1 17
HELIX 16 16 THR A 420 PHE A 432 1 13
HELIX 17 17 LYS A 435 ASN A 440 1 6
HELIX 18 18 ASP A 443 SER A 450 1 8
HELIX 19 19 THR A 465 ALA A 478 1 14
HELIX 20 20 LYS A 479 PHE A 486 5 8
HELIX 21 21 ASN A 487 LYS A 492 5 6
HELIX 22 22 SER A 495 ARG A 509 1 15
HELIX 23 23 PRO A 513 ASN A 525 1 13
HELIX 24 24 PHE A 526 ILE A 529 5 4
HELIX 25 25 ASN A 531 SER A 545 1 15
HELIX 26 26 TRP A 547 ASP A 549 5 3
HELIX 27 27 ALA A 550 GLN A 561 1 12
HELIX 28 28 ARG A 563 PHE A 577 1 15
HELIX 29 29 SER A 580 LYS A 592 1 13
HELIX 30 30 HIS A 596 LYS A 608 1 13
SHEET 1 A 8 GLN A 69 GLU A 70 0
SHEET 2 A 8 LEU A 59 ILE A 66 -1 N ILE A 66 O GLN A 69
SHEET 3 A 8 GLU A 99 THR A 108 -1 O GLU A 103 N VAL A 65
SHEET 4 A 8 THR A 33 SER A 44 -1 N ALA A 38 O ILE A 104
SHEET 5 A 8 CYS A 16 ASP A 28 -1 N LYS A 19 O THR A 41
SHEET 6 A 8 LEU A 154 PRO A 163 1 O GLU A 159 N LEU A 23
SHEET 7 A 8 ARG A 186 ILE A 197 -1 O PHE A 191 N ALA A 158
SHEET 8 A 8 ILE A 173 PRO A 179 -1 N THR A 178 O ILE A 188
SHEET 1 B 3 LEU A 49 LEU A 54 0
SHEET 2 B 3 MET A 86 LEU A 94 -1 O LEU A 94 N LEU A 49
SHEET 3 B 3 TYR A 73 LEU A 75 -1 N ALA A 74 O GLU A 87
SHEET 1 C 4 LEU A 115 LEU A 118 0
SHEET 2 C 4 TYR A 130 SER A 133 -1 O TYR A 130 N LEU A 118
SHEET 3 C 4 LEU A 204 GLY A 207 -1 O VAL A 206 N LEU A 131
SHEET 4 C 4 VAL A 167 MET A 170 -1 N VAL A 167 O GLY A 207
SHEET 1 D 5 GLU A 210 GLY A 215 0
SHEET 2 D 5 THR A 218 SER A 222 -1 O VAL A 220 N ARG A 212
SHEET 3 D 5 ASP A 257 VAL A 260 1 O LEU A 258 N TRP A 221
SHEET 4 D 5 LEU A 275 VAL A 278 1 O THR A 276 N LEU A 259
SHEET 5 D 5 GLY A 269 MET A 270 -1 N MET A 270 O PHE A 277
SHEET 1 E 2 VAL A 306 ASN A 308 0
SHEET 2 E 2 LYS A 417 ILE A 419 1 O ILE A 419 N THR A 307
LINK NE2 HIS A 295 ZN ZN A 701 1555 1555 2.07
LINK NE2 HIS A 299 ZN ZN A 701 1555 1555 2.10
LINK OE1 GLU A 318 ZN ZN A 701 1555 1555 1.98
LINK OD1 ASP A 426 YB YB A 801 1555 4457 2.15
CISPEP 1 GLN A 136 ALA A 137 0 1.15
CISPEP 2 ALA A 510 PRO A 511 0 0.14
SITE 1 AC1 4 HIS A 295 HIS A 299 GLU A 318 TYR A 383
SITE 1 AC2 4 ASP A 422 ASP A 426 ASP A 481 HOH A1274
SITE 1 AC3 3 LYS A 425 ASP A 426 ASP A 481
SITE 1 AC4 6 GLY A 344 GLY A 347 GLU A 348 GLU A 501
SITE 2 AC4 6 ALA A 504 GLN A 508
SITE 1 AC5 11 GLN A 134 GLN A 136 TYR A 267 GLU A 271
SITE 2 AC5 11 TRP A 311 PHE A 314 GLU A 318 PRO A 374
SITE 3 AC5 11 ALA A 377 TYR A 378 TYR A 383
CRYST1 67.767 133.572 83.629 90.00 90.00 90.00 P 21 21 2 4
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 0.014756 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007487 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011958 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
