Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6HGQ

Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+

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
B	0002055	molecular_function	adenine binding
B	0003999	molecular_function	adenine phosphoribosyltransferase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006166	biological_process	purine ribonucleoside salvage
B	0006168	biological_process	adenine salvage
B	0007625	biological_process	grooming behavior
B	0016208	molecular_function	AMP binding
B	0016757	molecular_function	glycosyltransferase activity
B	0032263	biological_process	GMP salvage
B	0032264	biological_process	IMP salvage
B	0034774	cellular_component	secretory granule lumen
B	0044209	biological_process	AMP salvage
B	0046083	biological_process	adenine metabolic process
B	0070062	cellular_component	extracellular exosome
C	0002055	molecular_function	adenine binding
C	0003999	molecular_function	adenine phosphoribosyltransferase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006166	biological_process	purine ribonucleoside salvage
C	0006168	biological_process	adenine salvage
C	0007625	biological_process	grooming behavior
C	0016208	molecular_function	AMP binding
C	0016757	molecular_function	glycosyltransferase activity
C	0032263	biological_process	GMP salvage
C	0032264	biological_process	IMP salvage
C	0034774	cellular_component	secretory granule lumen
C	0044209	biological_process	AMP salvage
C	0046083	biological_process	adenine metabolic process
C	0070062	cellular_component	extracellular exosome
D	0002055	molecular_function	adenine binding
D	0003999	molecular_function	adenine phosphoribosyltransferase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006166	biological_process	purine ribonucleoside salvage
D	0006168	biological_process	adenine salvage
D	0007625	biological_process	grooming behavior
D	0016208	molecular_function	AMP binding
D	0016757	molecular_function	glycosyltransferase activity
D	0032263	biological_process	GMP salvage
D	0032264	biological_process	IMP salvage
D	0034774	cellular_component	secretory granule lumen
D	0044209	biological_process	AMP salvage
D	0046083	biological_process	adenine metabolic process
D	0070062	cellular_component	extracellular exosome

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	4
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
C	ALA2
D	ALA2
B	ALA2

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
B	SER4
A	SER4
C	SER4
D	SER4

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER15
A	SER15
C	SER15
D	SER15

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
D	SER30
B	SER30
A	SER30
C	SER30

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
D	TYR60
B	TYR60
A	TYR60
C	TYR60

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER66
C	SER66
D	SER66
B	SER66

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS114
C	LYS114
D	LYS114
B	LYS114

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
A	THR135
C	THR135
D	THR135
B	THR135

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)