Structure of PDB 4zht Chain B Binding Site BS02

Receptor Information
>4zht Chain B (length=382) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNT
YRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIM
IVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYH
VCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGD
DVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAG
SKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVRE
VGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPC
SKIYGDGNAVPRILKFLKSIDLQEPLQKKFCF
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 B 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 F251 K259 V262 E271 V279 K280 H281
Binding residue
(residue number reindexed from 1)		D46 F244 K252 V255 E264 V272 K273 H274
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D112 E134 D143 H220 V222 I254
Catalytic site (residue number reindexed from 1) D105 E127 D136 H213 V215 I247
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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