Structure of PDB 4zht Chain D

Receptor sequence
>4zhtD (length=383) Species: 9606 (Homo sapiens) [Search protein sequence]
RKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNT
YRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIM
IVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYH
VCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGD
DVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAG
SKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVRE
VGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPC
SKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFP
3D structure
PDB4zht Mechanism and inhibition of human UDP-GlcNAc 2-epimerase, the key enzyme in sialic acid biosynthesis.
ChainD
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 UDP D R19 S23 R113 H220 N253 H281 V282 F284 F287 S301 S302 E307 R321 R12 S16 R106 H213 N246 H274 V275 F277 F280 S294 S295 E300 R314
BS02 NCC D D53 K259 V262 E271 V279 K280 H281 D46 K252 V255 E264 V272 K273 H274
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

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Molecular Function
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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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