Structure of PDB 1hzj Chain B Binding Site BS02

Receptor Information
>1hzj 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
GCTNPYGKSKFFIEEMIRDLCQADKTWNVVLLRYFNPTGAHASGCIGEDP
QGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGH
IAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARRE
GDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGT
Ligand information
Ligand IDUD1
InChIInChI=1S/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11-,12-,13-,14-,15-,16-/m1/s1
InChIKeyLFTYTUAZOPRMMI-CFRASDGPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)NC1C(C(C(OC1OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
CACTVS 3.341CC(=O)N[CH]1[CH](O)[CH](O)[CH](CO)O[CH]1O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1NC(=O)C)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
CACTVS 3.341CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[P@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O
OpenEye OEToolkits 1.5.0CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
FormulaC17 H27 N3 O17 P2
NameURIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
ChEMBLCHEMBL388154
DrugBankDB03397
ZINCZINC000008551100
PDB chain1hzj 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

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PDB1hzj Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		K92 S132 Y157 F186 N187 N206 N207 L208 N224 F226 R239 R300 D303
Binding residue
(residue number reindexed from 1)		K91 S131 Y156 F185 N186 N205 N206 L207 N223 F225 R238 R299 D302
Annotation score3
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hzj, PDBe:1hzj, PDBj:1hzj
PDBsum1hzj
PubMed11279032
UniProtQ14376|GALE_HUMAN UDP-glucose 4-epimerase (Gene Name=GALE)

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