Structure of PDB 4zht Chain B

Receptor sequence

>4zhtB (length=382) Species: 9606 (Homo sapiens)

RKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNT
YRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIM
IVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYH
VCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGD
DVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAG
SKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVRE
VGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPC
SKIYGDGNAVPRILKFLKSIDLQEPLQKKFCF

3D structure

• PDB: 4zht Mechanism and inhibition of human UDP-GlcNAc 2-epimerase, the key enzyme in sialic acid biosynthesis.
• Chain: B
• Resolution: 2.69 Å

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	B	R19 A20 S23 R113 L218 H220 H281 V282 F284 F287 S301 S302 E307 R321	R12 A13 S16 R106 L211 H213 H274 V275 F277 F280 S294 S295 E300 R314
BS02	NCC	B	D53 F251 K259 V262 E271 V279 K280 H281	D46 F244 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

External links

• PDB: RCSB:4zht, PDBe:4zht, PDBj:4zht
• PDBsum: 4zht
• PubMed: 26980148
• UniProt: Q9Y223|GLCNE_HUMAN Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (Gene Name=GNE)