HEADER OXIDOREDUCTASE 18-MAR-15 4YU1
TITLE HUMAN ALDOSE REDUCTASE COMPLEXED WITH SCHL12134 (3-[5-(3-NITROPHENYL)-
TITLE 2 2-THIENYL]PROPANOIC ACID) AT 1.02 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AR,ALDEHYDE REDUCTASE,ALDO-KETO REDUCTASE FAMILY 1 MEMBER
COMPND 5 B1;
COMPND 6 EC: 1.1.1.21;
COMPND 7 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: AKR1B1, ALDR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS TIM-BARREL, OXIDOREDUCTASE, PROTEIN-LIGAND-COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.RECHLIN,A.HEINE,G.KLEBE
REVDAT 2 10-JAN-24 4YU1 1 REMARK
REVDAT 1 23-MAR-16 4YU1 0
JRNL AUTH C.RECHLIN,A.HEINE,R.ORTMANN,M.SCHLITZER,G.KLEBE
JRNL TITL KEYS TO OPEN THE SPECIFICITY POCKET: BIPHENYLIC INHIBITORS
JRNL TITL 2 OF THE HUMAN ALDOSE REDUCTASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1492)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 150569
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.150
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7528
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.7117 - 3.1640 0.99 4977 262 0.1344 0.1569
REMARK 3 2 3.1640 - 2.5121 0.99 4931 259 0.1453 0.1635
REMARK 3 3 2.5121 - 2.1948 0.99 4915 259 0.1420 0.1483
REMARK 3 4 2.1948 - 1.9942 0.98 4871 256 0.1313 0.1418
REMARK 3 5 1.9942 - 1.8513 0.98 4866 257 0.1337 0.1547
REMARK 3 6 1.8513 - 1.7422 0.99 4902 258 0.1268 0.1292
REMARK 3 7 1.7422 - 1.6550 0.99 4856 255 0.1233 0.1279
REMARK 3 8 1.6550 - 1.5829 0.99 4891 258 0.1152 0.1318
REMARK 3 9 1.5829 - 1.5220 0.99 4876 256 0.1120 0.1312
REMARK 3 10 1.5220 - 1.4695 0.98 4851 255 0.1149 0.1419
REMARK 3 11 1.4695 - 1.4236 0.98 4841 255 0.1164 0.1256
REMARK 3 12 1.4236 - 1.3829 0.98 4811 253 0.1137 0.1534
REMARK 3 13 1.3829 - 1.3465 0.98 4837 255 0.1153 0.1387
REMARK 3 14 1.3465 - 1.3136 0.98 4772 251 0.1132 0.1327
REMARK 3 15 1.3136 - 1.2838 0.97 4802 253 0.1166 0.1340
REMARK 3 16 1.2838 - 1.2564 0.97 4780 251 0.1154 0.1347
REMARK 3 17 1.2564 - 1.2313 0.97 4767 251 0.1153 0.1469
REMARK 3 18 1.2313 - 1.2081 0.96 4725 249 0.1187 0.1497
REMARK 3 19 1.2081 - 1.1865 0.96 4739 250 0.1195 0.1286
REMARK 3 20 1.1865 - 1.1664 0.96 4753 250 0.1187 0.1437
REMARK 3 21 1.1664 - 1.1476 0.96 4705 247 0.1215 0.1383
REMARK 3 22 1.1476 - 1.1299 0.95 4706 248 0.1261 0.1313
REMARK 3 23 1.1299 - 1.1133 0.95 4721 248 0.1402 0.1865
REMARK 3 24 1.1133 - 1.0976 0.96 4683 246 0.1550 0.1648
REMARK 3 25 1.0976 - 1.0828 0.95 4621 244 0.1554 0.1617
REMARK 3 26 1.0828 - 1.0687 0.95 4725 248 0.1673 0.1773
REMARK 3 27 1.0687 - 1.0554 0.95 4612 243 0.1864 0.1920
REMARK 3 28 1.0554 - 1.0426 0.94 4652 245 0.1973 0.2171
REMARK 3 29 1.0426 - 1.0305 0.94 4548 239 0.2095 0.2504
REMARK 3 30 1.0305 - 1.0189 0.87 4305 227 0.2353 0.2408
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.070
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2803
REMARK 3 ANGLE : 1.371 3852
REMARK 3 CHIRALITY : 0.088 428
REMARK 3 PLANARITY : 0.010 509
REMARK 3 DIHEDRAL : 13.856 1054
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208081.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150587
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2DUX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION SOLUTION: 50 MM DI
REMARK 280 -AMMONIUMHYDROGEN CITRATE PH 5.0 PEG6000= 5 % (M/V) DTT= 5.15 G/
REMARK 280 L NADP+= 0.66 G/L AND HUMAN ALDOSE REDUCTASE= 15 MG/
REMARK 280 ML.AFTERWARDS THE CRYSTALS WERE SOAKED INTO TRIS 100 MM 25% (M/V)
REMARK 280 PEG6000 PH 8.0 SATURATED WITH THE INHIBITOR., VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
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 33.17700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 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 68 CE NZ
REMARK 470 GLU A 70 CD OE1 OE2
REMARK 470 LYS A 85 CG CD CE NZ
REMARK 470 LYS A 116 NZ
REMARK 470 LYS A 119 CE NZ
REMARK 470 GLU A 126 CG CD OE1 OE2
REMARK 470 ASN A 136 CG OD1 ND2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 LYS A 221 CD CE NZ
REMARK 470 LYS A 234 NZ
REMARK 470 GLU A 267 CD OE1 OE2
REMARK 470 LEU A 301 CG CD1 CD2
REMARK 470 GLU A 313 CD OE1 OE2
REMARK 470 GLU A 314 CG CD OE1 OE2
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 GLY A 25 O - C - N ANGL. DEV. = -9.8 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 21 -2.75 78.81
REMARK 500 LEU A 190 80.48 -150.33
REMARK 500 ARG A 293 16.39 -143.85
REMARK 500 ALA A 299 118.91 -169.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 25 -18.95
REMARK 500 GLY A 25 -18.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 728 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 773 DISTANCE = 7.48 ANGSTROMS
REMARK 525 HOH A 782 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 783 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A 784 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A 787 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 789 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A 790 DISTANCE = 8.10 ANGSTROMS
REMARK 525 HOH A 791 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH A 792 DISTANCE = 10.05 ANGSTROMS
REMARK 525 HOH A 793 DISTANCE = 10.78 ANGSTROMS
REMARK 525 HOH A 806 DISTANCE = 8.46 ANGSTROMS
REMARK 525 HOH A 809 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH A 823 DISTANCE = 8.76 ANGSTROMS
REMARK 525 HOH A 848 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH A 851 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 859 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 864 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH A 882 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH A 895 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 906 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 911 DISTANCE = 6.04 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 53N A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IKG RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
REMARK 900 RELATED ID: 2IKH RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
REMARK 900 RELATED ID: 3DN5 RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
REMARK 900 RELATED ID: 4NKC RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
REMARK 900 RELATED ID: 4PR4 RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
REMARK 900 RELATED ID: 4PRR RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
REMARK 900 RELATED ID: 4PRT RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ANOTHER INHIBITOR FROM THE
REMARK 900 SAME GROUP.
DBREF 4YU1 A 0 315 UNP P15121 ALDR_HUMAN 1 316
SEQADV 4YU1 ILE A 4 UNP P15121 LEU 5 CONFLICT
SEQRES 1 A 316 MET ALA SER ARG ILE LEU LEU ASN ASN GLY ALA LYS MET
SEQRES 2 A 316 PRO ILE LEU GLY LEU GLY THR TRP LYS SER PRO PRO GLY
SEQRES 3 A 316 GLN VAL THR GLU ALA VAL LYS VAL ALA ILE ASP VAL GLY
SEQRES 4 A 316 TYR ARG HIS ILE ASP CYS ALA HIS VAL TYR GLN ASN GLU
SEQRES 5 A 316 ASN GLU VAL GLY VAL ALA ILE GLN GLU LYS LEU ARG GLU
SEQRES 6 A 316 GLN VAL VAL LYS ARG GLU GLU LEU PHE ILE VAL SER LYS
SEQRES 7 A 316 LEU TRP CYS THR TYR HIS GLU LYS GLY LEU VAL LYS GLY
SEQRES 8 A 316 ALA CYS GLN LYS THR LEU SER ASP LEU LYS LEU ASP TYR
SEQRES 9 A 316 LEU ASP LEU TYR LEU ILE HIS TRP PRO THR GLY PHE LYS
SEQRES 10 A 316 PRO GLY LYS GLU PHE PHE PRO LEU ASP GLU SER GLY ASN
SEQRES 11 A 316 VAL VAL PRO SER ASP THR ASN ILE LEU ASP THR TRP ALA
SEQRES 12 A 316 ALA MET GLU GLU LEU VAL ASP GLU GLY LEU VAL LYS ALA
SEQRES 13 A 316 ILE GLY ILE SER ASN PHE ASN HIS LEU GLN VAL GLU MET
SEQRES 14 A 316 ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO ALA VAL
SEQRES 15 A 316 ASN GLN ILE GLU CYS HIS PRO TYR LEU THR GLN GLU LYS
SEQRES 16 A 316 LEU ILE GLN TYR CYS GLN SER LYS GLY ILE VAL VAL THR
SEQRES 17 A 316 ALA TYR SER PRO LEU GLY SER PRO ASP ARG PRO TRP ALA
SEQRES 18 A 316 LYS PRO GLU ASP PRO SER LEU LEU GLU ASP PRO ARG ILE
SEQRES 19 A 316 LYS ALA ILE ALA ALA LYS HIS ASN LYS THR THR ALA GLN
SEQRES 20 A 316 VAL LEU ILE ARG PHE PRO MET GLN ARG ASN LEU VAL VAL
SEQRES 21 A 316 ILE PRO LYS SER VAL THR PRO GLU ARG ILE ALA GLU ASN
SEQRES 22 A 316 PHE LYS VAL PHE ASP PHE GLU LEU SER SER GLN ASP MET
SEQRES 23 A 316 THR THR LEU LEU SER TYR ASN ARG ASN TRP ARG VAL CYS
SEQRES 24 A 316 ALA LEU LEU SER CYS THR SER HIS LYS ASP TYR PRO PHE
SEQRES 25 A 316 HIS GLU GLU PHE
HET NAP A 401 48
HET 53N A 402 19
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM 53N 3-[5-(3-NITROPHENYL)THIOPHEN-2-YL]PROPANOIC ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 53N C13 H11 N O4 S
FORMUL 4 HOH *413(H2 O)
HELIX 1 AA1 PRO A 23 GLY A 38 1 16
HELIX 2 AA2 ALA A 45 GLN A 49 5 5
HELIX 3 AA3 ASN A 50 GLU A 64 1 15
HELIX 4 AA4 LYS A 68 LEU A 72 5 5
HELIX 5 AA5 TRP A 79 HIS A 83 5 5
HELIX 6 AA6 GLU A 84 GLY A 86 5 3
HELIX 7 AA7 LEU A 87 LYS A 100 1 14
HELIX 8 AA8 ASN A 136 GLU A 150 1 15
HELIX 9 AA9 ASN A 162 ASN A 171 1 10
HELIX 10 AB1 GLN A 192 LYS A 202 1 11
HELIX 11 AB2 SER A 226 GLU A 229 5 4
HELIX 12 AB3 ASP A 230 HIS A 240 1 11
HELIX 13 AB4 THR A 243 GLN A 254 1 12
HELIX 14 AB5 THR A 265 LYS A 274 1 10
HELIX 15 AB6 SER A 281 SER A 290 1 10
HELIX 16 AB7 LEU A 300 THR A 304 5 5
SHEET 1 AA1 2 ARG A 3 LEU A 5 0
SHEET 2 AA1 2 LYS A 11 PRO A 13 -1 O MET A 12 N ILE A 4
SHEET 1 AA2 8 LEU A 17 GLY A 18 0
SHEET 2 AA2 8 HIS A 41 ASP A 43 1 O ASP A 43 N LEU A 17
SHEET 3 AA2 8 PHE A 73 LEU A 78 1 O VAL A 75 N ILE A 42
SHEET 4 AA2 8 LEU A 106 ILE A 109 1 O LEU A 108 N LEU A 78
SHEET 5 AA2 8 ILE A 156 SER A 159 1 O GLY A 157 N ILE A 109
SHEET 6 AA2 8 VAL A 181 GLU A 185 1 O VAL A 181 N ILE A 158
SHEET 7 AA2 8 VAL A 205 TYR A 209 1 O THR A 207 N ILE A 184
SHEET 8 AA2 8 VAL A 258 VAL A 259 1 O VAL A 258 N ALA A 208
SITE 1 AC1 34 GLY A 18 THR A 19 TRP A 20 LYS A 21
SITE 2 AC1 34 ASP A 43 TYR A 48 LYS A 77 HIS A 110
SITE 3 AC1 34 TRP A 111 SER A 159 ASN A 160 GLN A 183
SITE 4 AC1 34 TYR A 209 SER A 210 PRO A 211 LEU A 212
SITE 5 AC1 34 GLY A 213 SER A 214 PRO A 215 ASP A 216
SITE 6 AC1 34 ALA A 245 ILE A 260 PRO A 261 LYS A 262
SITE 7 AC1 34 SER A 263 VAL A 264 THR A 265 ARG A 268
SITE 8 AC1 34 GLU A 271 ASN A 272 53N A 402 HOH A 520
SITE 9 AC1 34 HOH A 579 HOH A 807
SITE 1 AC2 12 TRP A 20 TYR A 48 HIS A 110 TRP A 111
SITE 2 AC2 12 THR A 113 CYS A 298 ALA A 299 LEU A 300
SITE 3 AC2 12 CYS A 303 TYR A 309 NAP A 401 HOH A 527
CRYST1 49.449 66.354 47.429 90.00 92.31 90.00 P 1 21 1 2
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 0.020223 0.000000 0.000815 0.00000
SCALE2 0.000000 0.015071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021101 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
