1O64

Crystal structure of an ATP phosphoribosyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0000166	molecular_function	nucleotide binding
A	0003879	molecular_function	ATP phosphoribosyltransferase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
B	0000105	biological_process	L-histidine biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0003879	molecular_function	ATP phosphoribosyltransferase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0008652	biological_process	amino acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 219

Chain	Residue
A	ARG45
A	PRO46
A	PHE47
B	LYS130

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 219

Chain	Residue
A	LYS130
B	ARG45
B	PRO46
B	PHE47

---

Functional Information from PROSITE/UniProt

site_id	PS01316
Number of Residues	22
Details	ATP_P_PHORIBOSYLTR ATP phosphoribosyltransferase signature. ElapiaGlSdlIvDIteTGrTL

Chain	Residue	Details
A	GLU134-LEU155

---