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6HGP

Crystal Structure of Human APRT wild type in complex with Phosphate ion.

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
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0034774cellular_componentsecretory granule lumen
A0044209biological_processAMP salvage
A0046083biological_processadenine metabolic process
A0070062cellular_componentextracellular exosome
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
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0034774cellular_componentsecretory granule lumen
B0044209biological_processAMP salvage
B0046083biological_processadenine metabolic process
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue PO4 A 200
ChainResidue
AALA131
ATHR132
AGLY133
AGLY134
ATHR135
AHOH329

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 B 200
ChainResidue
BGLY134
BTHR135
BHOH308
BALA131
BTHR132
BGLY133

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
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BSER4
ASER4

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER15
ASER15

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER30
BSER30

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR60
BTYR60

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER66
BSER66

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS114
BLYS114

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR135
BTHR135

220472

PDB entries from 2024-05-29

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