Structure of PDB 1a9z Chain A Binding Site BS02
Receptor Information
>1a9z Chain A (length=338) Species:
562
(Escherichia coli) [
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MRVLVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGK
HPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNN
VNGTLRLISAMRAANVKNFIFSSAATVYGDNPKIPYVESFPTGTPQSPFG
KSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNL
MPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKL
ANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYW
ADASKADRELNWRVTRTLDEMAQDTWHWQSRHPQGYPD
Ligand information
Ligand ID
UPG
InChI
InChI=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
InChIKey
HSCJRCZFDFQWRP-JZMIEXBBSA-N
SMILES
Software
SMILES
CACTVS 3.370
OC[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 12.01
O=C1C=CN(C(=O)N1)C2OC(C(O)C2O)COP(=O)(OP(=O)(OC3OC(C(O)C(O)C3O)CO)O)O
CACTVS 3.370
OC[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 1.7.6
C1=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 1.7.6
C1=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
Formula
C15 H24 N2 O17 P2
Name
URIDINE-5'-DIPHOSPHATE-GLUCOSE;
URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBL
CHEMBL375951
DrugBank
DB01861
ZINC
ZINC000008215472
PDB chain
1a9z Chain A Residue 341 [
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Receptor-Ligand Complex Structure
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PDB
1a9z
Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
A125 F149 Y177 F178 N179 N199 L200 A216 I217 F218 R231 Y233 R292 Y299
Binding residue
(residue number reindexed from 1)
A125 F149 Y177 F178 N179 N199 L200 A216 I217 F218 R231 Y233 R292 Y299
Annotation score
4
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1a9z
,
PDBe:1a9z
,
PDBj:1a9z
PDBsum
1a9z
PubMed
9708982
UniProt
P09147
|GALE_ECOLI UDP-glucose 4-epimerase (Gene Name=galE)
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