2YQH

Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the substrate-binding form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0070569	molecular_function	uridylyltransferase activity
B	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0070569	molecular_function	uridylyltransferase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9M9P3

Chain	Residue	Details
B	GLN199
B	GLY226
B	ASP257
B	LYS389
A	MET109
A	LYS123
A	GLN199
A	GLY226
A	ASP257
A	LYS389
B	MET109
B	LYS123

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
B	ASN227
B	LYS421
A	ASN227
A	LYS421

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