Structure of PDB 1ek6 Chain B Binding Site BS02

Receptor Information
>1ek6 Chain B (length=345) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRR
VQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKP
LDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTG
GCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDP
QGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGH
IAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARRE
GDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGT
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 chain1ek6 Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1ek6 Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		K92 S132 Y157 F186 N187 N206 N207 L208 N224 V225 F226 R239 V277 R300 D303
Binding residue
(residue number reindexed from 1)		K91 S131 Y156 F185 N186 N205 N206 L207 N223 V224 F225 R238 V276 R299 D302
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S132 A133 T134 Y157 K161
Catalytic site (residue number reindexed from 1) S131 A132 T133 Y156 K160
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
5.1.3.7: UDP-N-acetylglucosamine 4-epimerase.
Gene Ontology
Molecular Function
GO:0003974 UDP-N-acetylglucosamine 4-epimerase activity
GO:0003978 UDP-glucose 4-epimerase activity
GO:0016853 isomerase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006012 galactose metabolic process
GO:0019388 galactose catabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ek6, PDBe:1ek6, PDBj:1ek6
PDBsum1ek6
PubMed10801319
UniProtQ14376|GALE_HUMAN UDP-glucose 4-epimerase (Gene Name=GALE)

[Back to BioLiP]