1DGM
CRYSTAL STRUCTURE OF ADENOSINE KINASE FROM TOXOPLASMA GONDII
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004001 | molecular_function | adenosine kinase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0016301 | molecular_function | kinase activity |
| A | 0044209 | biological_process | AMP salvage |
| A | 0055086 | biological_process | nucleobase-containing small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 380 |
| Chain | Residue |
| A | ALA185 |
| A | ILE188 |
| A | ALA191 |
| A | HOH406 |
| A | HOH471 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 385 |
| Chain | Residue |
| A | ASN20 |
| A | ALA71 |
| A | THR167 |
| A | ADN375 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADN A 375 |
| Chain | Residue |
| A | ASN20 |
| A | ASP24 |
| A | GLY69 |
| A | SER70 |
| A | LEU138 |
| A | TYR169 |
| A | ASP318 |
| A | CL385 |
| A | HOH416 |
| A | HOH517 |
| A | HOH536 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 370 |
| Chain | Residue |
| A | GLY315 |
| A | ALA316 |
| A | GLY317 |
| A | ASP318 |
Functional Information from PROSITE/UniProt
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTnGAGDafvGGFL |
| Chain | Residue | Details |
| A | ASP312-LEU325 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10794412","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10669608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LII","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10794412","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | ARG136 | |
| A | ASP318 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | ALA316 | |
| A | GLY317 | |
| A | GLY315 | |
| A | ASP318 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 209 |
| Chain | Residue | Details |
| A | ARG136 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP318 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
