5OAT
PINK1 structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | ASP359 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| B | ASP359 |
| C | ASP229 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | ASP229 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue MG E 602 |
| Chain | Residue |
| E | ASP359 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue MG F 601 |
| Chain | Residue |
| D | ASP359 |
| F | ASP229 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKsdNLLL |
| Chain | Residue | Details |
| A | ILE333-LEU345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YJ9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YJ9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"22645651","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28980524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29475881","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
