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	0019276	biological_process	UDP-N-acetylgalactosamine metabolic process
A	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase 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	0019276	biological_process	UDP-N-acetylgalactosamine metabolic process
B	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
B	0070569	molecular_function	uridylyltransferase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Motif: {"description":"Substrate binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9M9P3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---