5YJ9
Crystal structure of Tribolium castaneum PINK1 kinase domain in complex with AMP-PNP
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue ANP D 601 |
| Chain | Residue |
| D | ALA169 |
| D | ASN342 |
| D | LEU344 |
| D | ASP359 |
| D | LYS446 |
| D | ASP449 |
| D | MG602 |
| D | MG603 |
| D | HOH701 |
| D | HOH702 |
| D | ALA194 |
| D | LYS196 |
| D | GLU217 |
| D | MSE294 |
| D | LYS295 |
| D | TYR297 |
| D | ASN300 |
| D | ASP341 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 602 |
| Chain | Residue |
| D | GLU217 |
| D | ASP359 |
| D | ANP601 |
| D | HOH703 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 603 |
| Chain | Residue |
| D | ASN342 |
| D | ASP359 |
| D | ANP601 |
| D | HOH701 |
| D | HOH702 |
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 |
| D | ILE333-LEU345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 | 6 |
| 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 | 1 |
| 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 | 1 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"29991771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
