2YQC

Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the apo-like 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 1201

Chain	Residue
A	ASN74
A	THR77
A	HOH1736
A	HOH1737

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1301

Chain	Residue
A	HOH1505
A	ILE195
A	PHE196
A	ASN237
A	HOH1312
A	HOH1483

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9M9P3

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

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS421
A	ASN227

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