Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6HGQ

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0002055molecular_functionadenine binding
A0003999molecular_functionadenine phosphoribosyltransferase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0006168biological_processadenine salvage
A0007625biological_processgrooming behavior
A0016208molecular_functionAMP binding
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0034774cellular_componentsecretory granule lumen
A0044209biological_processAMP salvage
A0046083biological_processadenine metabolic process
A0070062cellular_componentextracellular exosome
A1901363molecular_functionheterocyclic compound binding
B0002055molecular_functionadenine binding
B0003999molecular_functionadenine phosphoribosyltransferase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006166biological_processpurine ribonucleoside salvage
B0006168biological_processadenine salvage
B0007625biological_processgrooming behavior
B0016208molecular_functionAMP binding
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0034774cellular_componentsecretory granule lumen
B0044209biological_processAMP salvage
B0046083biological_processadenine metabolic process
B0070062cellular_componentextracellular exosome
B1901363molecular_functionheterocyclic compound binding
C0002055molecular_functionadenine binding
C0003999molecular_functionadenine phosphoribosyltransferase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006166biological_processpurine ribonucleoside salvage
C0006168biological_processadenine salvage
C0007625biological_processgrooming behavior
C0016208molecular_functionAMP binding
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0032263biological_processGMP salvage
C0032264biological_processIMP salvage
C0034774cellular_componentsecretory granule lumen
C0044209biological_processAMP salvage
C0046083biological_processadenine metabolic process
C0070062cellular_componentextracellular exosome
C1901363molecular_functionheterocyclic compound binding
D0002055molecular_functionadenine binding
D0003999molecular_functionadenine phosphoribosyltransferase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006166biological_processpurine ribonucleoside salvage
D0006168biological_processadenine salvage
D0007625biological_processgrooming behavior
D0016208molecular_functionAMP binding
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0032263biological_processGMP salvage
D0032264biological_processIMP salvage
D0034774cellular_componentsecretory granule lumen
D0044209biological_processAMP salvage
D0046083biological_processadenine metabolic process
D0070062cellular_componentextracellular exosome
D1901363molecular_functionheterocyclic compound binding
Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVVVDDLLATGgT
ChainResidueDetails
AVAL123-THR135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"12665801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified 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"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon