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	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

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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712

Chain	Residue	Details
A	ALA2

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER4

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER15

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER30

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR60

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER66

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS114

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR135

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