Structure of PDB 1kvr Chain A Binding Site BS01

Receptor Information
>1kvr Chain A (length=338) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRVLVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGK
HPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNN
VNGTLRLISAMRAANVKNFIFSSAATVYGDQPKIPYVESFPTGTPQSPYG
KSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNL
MPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKL
ANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYW
ADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain1kvr Chain A Residue 340 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1kvr Molecular structures of the S124A, S124T, and S124V site-directed mutants of UDP-galactose 4-epimerase from Escherichia coli.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G7 G10 Y11 I12 D31 N32 C34 N35 S36 D58 I59 F80 A81 G82 K84 S122 S123 Y149 K153 Y177 P180
Binding residue
(residue number reindexed from 1)		G7 G10 Y11 I12 D31 N32 C34 N35 S36 D58 I59 F80 A81 G82 K84 S122 S123 Y149 K153 Y177 P180
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) A124 A125 T126 Y149 K153 M189
Catalytic site (residue number reindexed from 1) A124 A125 T126 Y149 K153 M189
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
Gene Ontology
Molecular Function
GO:0003978 UDP-glucose 4-epimerase activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
GO:0042802 identical protein binding
GO:0070403 NAD+ binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006012 galactose metabolic process
GO:0009242 colanic acid biosynthetic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1kvr, PDBe:1kvr, PDBj:1kvr
PDBsum1kvr
PubMed9271499
UniProtP09147|GALE_ECOLI UDP-glucose 4-epimerase (Gene Name=galE)

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