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	0019276	biological_process	UDP-N-acetylgalactosamine metabolic process
A	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase 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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Motif: {"description":"Substrate binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9M9P3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---