1ZN8
Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution
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 | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1030 |
| Chain | Residue |
| B | TRP98 |
| B | ARG145 |
| B | HOH1211 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP A 1031 |
| Chain | Residue |
| A | LEU129 |
| A | ALA131 |
| A | THR132 |
| A | GLY133 |
| A | GLY134 |
| A | THR135 |
| A | LEU159 |
| A | HOH1032 |
| A | HOH1033 |
| A | HOH1034 |
| A | HOH1061 |
| A | HOH1093 |
| A | HOH1114 |
| A | HOH1158 |
| A | VAL25 |
| A | PHE26 |
| A | ARG27 |
| A | ARG67 |
| A | ASP127 |
| A | ASP128 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AMP B 1032 |
| Chain | Residue |
| B | VAL25 |
| B | PHE26 |
| B | ARG27 |
| B | ARG67 |
| B | ASP127 |
| B | ASP128 |
| B | ALA131 |
| B | THR132 |
| B | GLY133 |
| B | GLY134 |
| B | THR135 |
| B | LEU159 |
| B | HOH1033 |
| B | HOH1034 |
| B | HOH1068 |
| B | HOH1084 |
| B | HOH1127 |
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 | 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 | ASP3 | |
| B | ASP3 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | GLU5 | |
| B | GLU5 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PHE16 | |
| B | PHE16 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PRO31 | |
| B | PRO31 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | ILE61 | |
| B | ILE61 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | ARG67 | |
| B | ARG67 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | ASP115 | |
| B | ASP115 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | MET136 | |
| B | MET136 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oro |
| Chain | Residue | Details |
| A | LYS91 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oro |
| Chain | Residue | Details |
| B | LYS91 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oro |
| Chain | Residue | Details |
| A | GLU104 | |
| A | ARG67 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oro |
| Chain | Residue | Details |
| B | GLU104 | |
| B | ARG67 |
