4X44

Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002055	molecular_function	adenine binding
A	0003999	molecular_function	adenine phosphoribosyltransferase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006166	biological_process	purine ribonucleoside salvage
A	0006168	biological_process	adenine salvage
A	0007625	biological_process	grooming behavior
A	0016208	molecular_function	AMP binding
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0032263	biological_process	GMP salvage
A	0032264	biological_process	IMP salvage
A	0034774	cellular_component	secretory granule lumen
A	0044209	biological_process	AMP salvage
A	0046083	biological_process	adenine metabolic process
A	0070062	cellular_component	extracellular exosome
A	1901363	molecular_function	heterocyclic compound binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue AMP A 1001

Chain	Residue
A	VAL25
A	GLY133
A	GLY134
A	THR135
A	LEU159
A	GOL1003
A	HOH1188
A	HOH1193
A	HOH1209
A	HOH1210
A	HOH1243
A	PHE26
A	ARG27
A	ARG67
A	ASP127
A	ASP128
A	LEU129
A	ALA131
A	THR132

---

site_id	AC2
Number of Residues	9
Details	binding site for residue SO4 A 1002

Chain	Residue
A	SER66
A	ARG67
A	ARG87
A	LYS91
A	HOH1102
A	HOH1123
A	HOH1135
A	HOH1152
A	HOH1259

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 1003

Chain	Residue
A	LEU103
A	LYS107
A	THR132
A	THR135
A	AMP1001
A	HOH1218

---

Functional Information from PROSITE/UniProt

site_id	PS00103
Number of Residues	13
Details	PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVVVDDLLATGgT

Chain	Residue	Details
A	VAL123-THR135

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---