6HGP
Crystal Structure of Human APRT wild type in complex with Phosphate ion.
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 |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 1901363 | molecular_function | heterocyclic compound binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 200 |
| Chain | Residue |
| A | ALA131 |
| A | THR132 |
| A | GLY133 |
| A | GLY134 |
| A | THR135 |
| A | HOH329 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 200 |
| Chain | Residue |
| B | GLY134 |
| B | THR135 |
| B | HOH308 |
| B | ALA131 |
| B | THR132 |
| B | GLY133 |
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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
