Structure of PDB 4koa Chain A Binding Site BS01

Receptor Information
>4koa Chain A (length=333) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIRWGLIGASTIAREWVIGAIRAAGGEVVSVMSSSAERGEAYAAENGIAK
AVTSVDDLVGDPDVDAVYISTTNELHHGQALAAIRAGKHVLCEKPLAMNL
NDGCEMVLKACEAGVVLGTNHHLRNAATHRAMREAIAAGRIGRPIAARVF
HAVYLPPHLQGWRLDKPEAGGGVILDITVHDADTLRFVLNDDPIEAVAIS
HSAGMGKEGLEDGVMGVLRFRSGVIAQFHDAFTTKFAETGLEVHGTAGSL
IGRNVMTQRPVGTVVLRNEEGESELPLDHRNLYETAIAAFHSAIGGNGRP
SASGEDGVWSLATGLAVVKAAATGGAVEIETGL
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain4koa Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4koa The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation.
Resolution1.93 Å
Binding residue
(original residue number in PDB)		G8 A9 S10 T11 I12 S33 S34 R38 T71 N73 H76 K94 Q160
Binding residue
(residue number reindexed from 1)		G8 A9 S10 T11 I12 S33 S34 R38 T71 N73 H76 K94 Q160
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) K94 H180
Catalytic site (residue number reindexed from 1) K94 H180
Enzyme Commision number 1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming).
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0033712 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:4koa, PDBe:4koa, PDBj:4koa
PDBsum4koa
PubMed23908025
UniProtQ92KZ3|AFR_RHIME 1,5-anhydro-D-fructose reductase (Gene Name=afr)

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