HEADER LYASE/LYASE INHIBITOR 29-MAY-13 4KYH
TITLE CRYSTAL STRUCTURE OF MOUSE GLYOXALASE I COMPLEXED WITH ZOPOLRESTAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTOYLGLUTATHIONE LYASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALDOKETOMUTASE, GLYOXALASE I, GLX I, KETONE-ALDEHYDE MUTASE,
COMPND 5 METHYLGLYOXALASE, S-D-LACTOYLGLUTATHIONE METHYLGLYOXAL LYASE;
COMPND 6 EC: 4.4.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GLO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS LACTOYLGLUTACHIONE LYASE, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHAI,M.YUAN,L.ZHANG,Y.CHEN,H.ZHANG,S.CHEN,Y.ZHAO
REVDAT 4 29-MAY-24 4KYH 1 REMARK
REVDAT 3 24-AUG-22 4KYH 1 JRNL REMARK LINK
REVDAT 2 04-DEC-19 4KYH 1 REMARK
REVDAT 1 07-AUG-13 4KYH 0
JRNL AUTH J.ZHAI,H.ZHANG,L.ZHANG,Y.ZHAO,S.CHEN,Y.CHEN,X.PENG,Q.LI,
JRNL AUTH 2 M.YUAN,X.HU
JRNL TITL ZOPOLRESTAT AS A HUMAN GLYOXALASE I INHIBITOR AND ITS
JRNL TITL 2 STRUCTURAL BASIS.
JRNL REF CHEMMEDCHEM V. 8 1462 2013
JRNL REFN ESSN 1860-7187
JRNL PMID 23857942
JRNL DOI 10.1002/CMDC.201300243
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 11001
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 552
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 797
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2788
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.315
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.217
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.607
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2901 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3937 ; 1.731 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 353 ; 6.757 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;40.733 ;24.962
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 485 ;16.165 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;13.040 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 420 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2320 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1774 ; 0.768 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2859 ; 1.403 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1127 ; 1.905 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1078 ; 2.933 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4KYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000079953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MULTILAYER OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05750
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18120
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 2000, 50MM MES, 0.1M NACL, PH
REMARK 280 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.35800
REMARK 290 SMTRY3 2 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: 8140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 PRO A 4
REMARK 465 GLN A 5
REMARK 465 ILE A 183
REMARK 465 ILE A 184
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 PRO B 4
REMARK 465 GLN B 5
REMARK 465 PRO B 6
REMARK 465 ALA B 7
REMARK 465 SER B 8
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 LYS A 85 CG CD CE NZ
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE ARG A 123 O HOH A 343 2.03
REMARK 500 O ASP B 154 NZ LYS B 159 2.11
REMARK 500 OE2 GLU B 143 O HOH B 241 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 161 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
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 179 43.23 -146.41
REMARK 500 ALA A 181 2.06 -65.41
REMARK 500 THR B 50 -62.45 -94.11
REMARK 500 ASP B 84 109.09 -56.05
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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 34 NE2
REMARK 620 2 GLU A 100 OE1 75.2
REMARK 620 3 HIS B 127 NE2 83.6 114.9
REMARK 620 4 GLU B 173 OE2 84.3 150.3 83.1
REMARK 620 5 HOH B 249 O 107.7 95.4 149.6 70.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 127 NE2
REMARK 620 2 GLU A 173 OE2 85.2
REMARK 620 3 GLN B 34 NE2 88.3 78.5
REMARK 620 4 GLU B 100 OE1 93.3 168.2 89.8
REMARK 620 5 HOH B 238 O 105.8 90.1 161.1 101.6
REMARK 620 N 1 2 3 4
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZST A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE GLYOXALASE I COMPLEXED WITH METHYL-
REMARK 900 GERFELIN
REMARK 900 RELATED ID: 4KYK RELATED DB: PDB
DBREF 4KYH A 1 184 UNP Q9CPU0 LGUL_MOUSE 1 184
DBREF 4KYH B 1 184 UNP Q9CPU0 LGUL_MOUSE 1 184
SEQRES 1 A 184 MET ALA GLU PRO GLN PRO ALA SER SER GLY LEU THR ASP
SEQRES 2 A 184 GLU THR ALA PHE SER CYS CYS SER ASP PRO ASP PRO SER
SEQRES 3 A 184 THR LYS ASP PHE LEU LEU GLN GLN THR MET LEU ARG ILE
SEQRES 4 A 184 LYS ASP PRO LYS LYS SER LEU ASP PHE TYR THR ARG VAL
SEQRES 5 A 184 LEU GLY LEU THR LEU LEU GLN LYS LEU ASP PHE PRO ALA
SEQRES 6 A 184 MET LYS PHE SER LEU TYR PHE LEU ALA TYR GLU ASP LYS
SEQRES 7 A 184 ASN ASP ILE PRO LYS ASP LYS SER GLU LYS THR ALA TRP
SEQRES 8 A 184 THR PHE SER ARG LYS ALA THR LEU GLU LEU THR HIS ASN
SEQRES 9 A 184 TRP GLY THR GLU ASP ASP GLU THR GLN SER TYR HIS ASN
SEQRES 10 A 184 GLY ASN SER ASP PRO ARG GLY PHE GLY HIS ILE GLY ILE
SEQRES 11 A 184 ALA VAL PRO ASP VAL TYR SER ALA CYS LYS ARG PHE GLU
SEQRES 12 A 184 GLU LEU GLY VAL LYS PHE VAL LYS LYS PRO ASP ASP GLY
SEQRES 13 A 184 LYS MET LYS GLY LEU ALA PHE ILE GLN ASP PRO ASP GLY
SEQRES 14 A 184 TYR TRP ILE GLU ILE LEU ASN PRO ASN LYS ILE ALA THR
SEQRES 15 A 184 ILE ILE
SEQRES 1 B 184 MET ALA GLU PRO GLN PRO ALA SER SER GLY LEU THR ASP
SEQRES 2 B 184 GLU THR ALA PHE SER CYS CYS SER ASP PRO ASP PRO SER
SEQRES 3 B 184 THR LYS ASP PHE LEU LEU GLN GLN THR MET LEU ARG ILE
SEQRES 4 B 184 LYS ASP PRO LYS LYS SER LEU ASP PHE TYR THR ARG VAL
SEQRES 5 B 184 LEU GLY LEU THR LEU LEU GLN LYS LEU ASP PHE PRO ALA
SEQRES 6 B 184 MET LYS PHE SER LEU TYR PHE LEU ALA TYR GLU ASP LYS
SEQRES 7 B 184 ASN ASP ILE PRO LYS ASP LYS SER GLU LYS THR ALA TRP
SEQRES 8 B 184 THR PHE SER ARG LYS ALA THR LEU GLU LEU THR HIS ASN
SEQRES 9 B 184 TRP GLY THR GLU ASP ASP GLU THR GLN SER TYR HIS ASN
SEQRES 10 B 184 GLY ASN SER ASP PRO ARG GLY PHE GLY HIS ILE GLY ILE
SEQRES 11 B 184 ALA VAL PRO ASP VAL TYR SER ALA CYS LYS ARG PHE GLU
SEQRES 12 B 184 GLU LEU GLY VAL LYS PHE VAL LYS LYS PRO ASP ASP GLY
SEQRES 13 B 184 LYS MET LYS GLY LEU ALA PHE ILE GLN ASP PRO ASP GLY
SEQRES 14 B 184 TYR TRP ILE GLU ILE LEU ASN PRO ASN LYS ILE ALA THR
SEQRES 15 B 184 ILE ILE
HET ZN A 201 1
HET ZN A 202 1
HET ZST A 203 29
HETNAM ZN ZINC ION
HETNAM ZST 3,4-DIHYDRO-4-OXO-3-((5-TRIFLUOROMETHYL-2-
HETNAM 2 ZST BENZOTHIAZOLYL)METHYL)-1-PHTHALAZINE ACETIC ACID
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 ZST C19 H12 F3 N3 O3 S
FORMUL 6 HOH *127(H2 O)
HELIX 1 1 THR A 12 CYS A 19 1 8
HELIX 2 2 ASP A 24 LYS A 28 5 5
HELIX 3 3 ASP A 41 VAL A 52 1 12
HELIX 4 4 ASP A 77 ILE A 81 5 5
HELIX 5 5 ASP A 84 PHE A 93 1 10
HELIX 6 6 GLY A 106 ASP A 110 5 5
HELIX 7 7 ASP A 134 LEU A 145 1 12
HELIX 8 8 ASN A 176 ILE A 180 5 5
HELIX 9 9 THR B 12 SER B 18 1 7
HELIX 10 10 ASP B 24 LYS B 28 5 5
HELIX 11 11 ASP B 41 VAL B 52 1 12
HELIX 12 12 ASP B 77 ILE B 81 5 5
HELIX 13 13 ASP B 84 PHE B 93 1 10
HELIX 14 14 GLY B 106 ASP B 110 5 5
HELIX 15 15 ASP B 134 LEU B 145 1 12
HELIX 16 16 ASN B 176 ILE B 184 1 9
SHEET 1 A 8 THR A 56 PHE A 63 0
SHEET 2 A 8 PHE A 68 ALA A 74 -1 O ALA A 74 N THR A 56
SHEET 3 A 8 THR A 98 ASN A 104 -1 O LEU A 101 N TYR A 71
SHEET 4 A 8 LEU A 31 ARG A 38 1 N THR A 35 O GLU A 100
SHEET 5 A 8 PHE B 125 ALA B 131 -1 O HIS B 127 N MET A 36
SHEET 6 A 8 TRP B 171 LEU B 175 1 O GLU B 173 N ILE B 130
SHEET 7 A 8 ALA B 162 GLN B 165 -1 N ILE B 164 O ILE B 172
SHEET 8 A 8 LYS B 148 LYS B 151 -1 N VAL B 150 O PHE B 163
SHEET 1 B 8 PHE A 149 LYS A 151 0
SHEET 2 B 8 ALA A 162 GLN A 165 -1 O PHE A 163 N LYS A 151
SHEET 3 B 8 TRP A 171 LEU A 175 -1 O ILE A 174 N ALA A 162
SHEET 4 B 8 PHE A 125 ALA A 131 1 N ILE A 130 O GLU A 173
SHEET 5 B 8 LEU B 31 ARG B 38 -1 O MET B 36 N HIS A 127
SHEET 6 B 8 THR B 98 ASN B 104 1 O THR B 102 N LEU B 37
SHEET 7 B 8 PHE B 68 ALA B 74 -1 N TYR B 71 O LEU B 101
SHEET 8 B 8 THR B 56 PHE B 63 -1 N LEU B 58 O PHE B 72
LINK NE2 GLN A 34 ZN ZN A 201 1555 1555 2.01
LINK OE1 GLU A 100 ZN ZN A 201 1555 1555 2.09
LINK NE2 HIS A 127 ZN ZN A 202 1555 1555 2.36
LINK OE2 GLU A 173 ZN ZN A 202 1555 1555 1.96
LINK ZN ZN A 201 NE2 HIS B 127 1555 1555 2.11
LINK ZN ZN A 201 OE2 GLU B 173 1555 1555 2.65
LINK ZN ZN A 201 O HOH B 249 1555 1555 2.59
LINK ZN ZN A 202 NE2 GLN B 34 1555 1555 1.96
LINK ZN ZN A 202 OE1 GLU B 100 1555 1555 1.86
LINK ZN ZN A 202 O HOH B 238 1555 1555 2.43
CISPEP 1 ASP A 121 PRO A 122 0 1.47
CISPEP 2 ASP B 121 PRO B 122 0 -9.19
SITE 1 AC1 5 GLN A 34 GLU A 100 HIS B 127 GLU B 173
SITE 2 AC1 5 HOH B 249
SITE 1 AC2 5 HIS A 127 GLU A 173 GLN B 34 GLU B 100
SITE 2 AC2 5 HOH B 238
SITE 1 AC3 10 MET A 36 ARG A 38 PHE A 68 GLU A 100
SITE 2 AC3 10 THR A 102 ASN A 104 HOH A 326 HOH A 348
SITE 3 AC3 10 ARG B 123 LYS B 151
CRYST1 41.781 64.716 65.361 90.00 101.90 90.00 P 1 21 1 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 0.023934 0.000000 0.005044 0.00000
SCALE2 0.000000 0.015452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015636 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
