Structure of PDB 1a9y Chain A Binding Site BS02

Receptor Information
>1a9y 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
VNGTLRLISAMRAANVKNFIFSSAATVYGDQPKIPYVESFPTGTPQSPFG
KSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNL
MPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKL
ANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYW
ADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
Ligand information
Ligand IDUPG
InChIInChI=1S/C15H24N2O17P2/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25)/t5-,6-,8-,9-,10+,11-,12-,13-,14-/m1/s1
InChIKeyHSCJRCZFDFQWRP-JZMIEXBBSA-N
SMILES
SoftwareSMILES
CACTVS 3.370OC[C@H]1O[C@H](O[P](O)(=O)O[P](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 12.01O=C1C=CN(C(=O)N1)C2OC(C(O)C2O)COP(=O)(OP(=O)(OC3OC(C(O)C(O)C3O)CO)O)O
CACTVS 3.370OC[CH]1O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@](=O)(O)O[P@](=O)(O)O[C@@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O)O)O
OpenEye OEToolkits 1.7.6C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)CO)O)O)O)O)O
FormulaC15 H24 N2 O17 P2
NameURIDINE-5'-DIPHOSPHATE-GLUCOSE;
URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBLCHEMBL375951
DrugBankDB01861
ZINCZINC000008215472
PDB chain1a9y Chain A Residue 341 [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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PDB1a9y Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		A125 T126 N179 N199 L200 A216 I217 F218 R231 Y233 R292 D295 Y299
Binding residue
(residue number reindexed from 1)		A125 T126 N179 N199 L200 A216 I217 F218 R231 Y233 R292 D295 Y299
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) A124 A125 T126 F149 K153
Catalytic site (residue number reindexed from 1) A124 A125 T126 F149 K153
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:1a9y, PDBe:1a9y, PDBj:1a9y
PDBsum1a9y
PubMed9708982
UniProtP09147|GALE_ECOLI UDP-glucose 4-epimerase (Gene Name=galE)

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