Structure of PDB 1i3k Chain B Binding Site BS02

Receptor Information
>1i3k 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
VQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAMGESVQKP
LDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTG
GCTNPYGKSKFFIEEMIRDLCQADKTWNVVLLRYFNPTGAHASGCIGEDP
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 chain1i3k Chain B Residue 901 [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]
PDB1i3k Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		S132 F186 N187 N207 L208 N224 V225 F226 R239 Y241 V277 R300 D303
Binding residue
(residue number reindexed from 1)		S131 F185 N186 N206 L207 N223 V224 F225 R238 Y240 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:1i3k, PDBe:1i3k, PDBj:1i3k
PDBsum1i3k
PubMed11279193
UniProtQ14376|GALE_HUMAN UDP-glucose 4-epimerase (Gene Name=GALE)

[Back to BioLiP]