Structure of PDB 1udc Chain A Binding Site BS02

Receptor Information
>1udc 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
VNGTLRLISAMRAANVKNFIFSSSATVYGDQPKIPYVESFPTGTPQSPYG
KSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNL
MPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKL
ANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYW
ADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
Ligand information
Ligand IDUFM
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-NYYOCOOHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC[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
OpenEye OEToolkits 1.5.0C1=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
CACTVS 3.341OC[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
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1O)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
OpenEye OEToolkits 1.5.0C1=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-MANNOSE
ChEMBLCHEMBL227711
DrugBankDB02421
ZINC
PDB chain1udc Chain A Residue 341 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1udc Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli.
Resolution1.65 Å
Binding residue
(original residue number in PDB)		T126 Y149 N179 N199 L200 L215 A216 I217 F218 R231 Y233 V269 R292
Binding residue
(residue number reindexed from 1)		T126 Y149 N179 N199 L200 L215 A216 I217 F218 R231 Y233 V269 R292
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S124 A125 T126 Y149 K153 M189
Catalytic site (residue number reindexed from 1) S124 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
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Cellular Component
External links
PDB RCSB:1udc, PDBe:1udc, PDBj:1udc
PDBsum1udc
PubMed9174344
UniProtP09147|GALE_ECOLI UDP-glucose 4-epimerase (Gene Name=galE)

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