Structure of PDB 4zht Chain A Binding Site BS02

Receptor Information
>4zht Chain A (length=384) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGN
TYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDI
MIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHY
HVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLG
DDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDA
GSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVR
EVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYP
CSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFP
Ligand information
Ligand IDNCC
InChIInChI=1S/C20H31N4O16P/c1-7(26)22-12-8(27)4-20(18(32)33,39-16(12)13(29)9(28)5-25)40-41(35,36)37-6-10-14(30)15(31)17(38-10)24-3-2-11(21)23-19(24)34/h2-3,8-10,12-17,25,27-31H,4-6H2,1H3,(H,22,26)(H,32,33)(H,35,36)(H2,21,23,34)/t8-,9+,10+,12+,13+,14+,15+,16+,17+,20+/m0/s1
InChIKeyTXCIAUNLDRJGJZ-BILDWYJOSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)N[C@@H]1[C@H](C[C@](O[C@H]1[C@@H]([C@@H](CO)O)O)(C(=O)O)O[P@@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=NC3=O)N)O)O)O
CACTVS 3.341CC(=O)N[CH]1[CH](O)C[C](O[CH]1[CH](O)[CH](O)CO)(O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=NC3=O)N)C(O)=O
ACDLabs 10.04O=C(NC1C(O)CC(OC1C(O)C(O)CO)(OP(=O)(O)OCC3OC(N2C(=O)N=C(N)C=C2)C(O)C3O)C(=O)O)C
OpenEye OEToolkits 1.5.0CC(=O)NC1C(CC(OC1C(C(CO)O)O)(C(=O)O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=NC3=O)N)O)O)O
CACTVS 3.341CC(=O)N[C@@H]1[C@@H](O)C[C@@](O[C@H]1[C@H](O)[C@H](O)CO)(O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=NC3=O)N)C(O)=O
FormulaC20 H31 N4 O16 P
NameCYTIDINE-5'-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC ACID
ChEMBLCHEMBL1234647
DrugBankDB02485
ZINCZINC000008215638
PDB chain4zht Chain A Residue 502 [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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PDB4zht Mechanism and inhibition of human UDP-GlcNAc 2-epimerase, the key enzyme in sialic acid biosynthesis.
Resolution2.69 Å
Binding residue
(original residue number in PDB)		D53 K259 E271 A278 K280 H281
Binding residue
(residue number reindexed from 1)		D47 K253 E265 A272 K274 H275
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D112 E134 D143 H220 V222 I254
Catalytic site (residue number reindexed from 1) D106 E128 D137 H214 V216 I248
Enzyme Commision number 2.7.1.60: N-acylmannosamine kinase.
3.2.1.183: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing).
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008761 UDP-N-acetylglucosamine 2-epimerase activity
Biological Process
GO:0006047 UDP-N-acetylglucosamine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4zht, PDBe:4zht, PDBj:4zht
PDBsum4zht
PubMed26980148
UniProtQ9Y223|GLCNE_HUMAN Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (Gene Name=GNE)

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