6R5F
Crystal structure of RIP1 kinase in complex with DHP77
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue JSW A 301 |
| Chain | Residue |
| A | ILE43 |
| A | VAL134 |
| A | HIS136 |
| A | ILE154 |
| A | ALA155 |
| A | ASP156 |
| A | LEU157 |
| A | LEU159 |
| A | SER161 |
| A | PHE162 |
| A | MET44 |
| A | LYS45 |
| A | MET67 |
| A | LEU70 |
| A | VAL76 |
| A | LEU78 |
| A | MET92 |
| A | LEU129 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue JSW B 301 |
| Chain | Residue |
| B | ILE43 |
| B | MET44 |
| B | LYS45 |
| B | MET67 |
| B | LEU70 |
| B | VAL76 |
| B | LEU78 |
| B | MET92 |
| B | LEU129 |
| B | HIS136 |
| B | ILE154 |
| B | ALA155 |
| B | ASP156 |
| B | LEU157 |
| B | LEU159 |
| B | SER161 |
| B | PHE162 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue JSW C 301 |
| Chain | Residue |
| C | LYS45 |
| C | MET67 |
| C | VAL76 |
| C | LEU90 |
| C | MET92 |
| C | LEU129 |
| C | HIS136 |
| C | ILE154 |
| C | ALA155 |
| C | ASP156 |
| C | SER161 |
| C | PHE162 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue JSW D 301 |
| Chain | Residue |
| D | LYS45 |
| D | MET67 |
| D | VAL75 |
| D | VAL76 |
| D | LEU78 |
| D | MET92 |
| D | ILE154 |
| D | ALA155 |
| D | ASP156 |
| D | LEU157 |
| D | PHE162 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHkDLKpeNILV |
| Chain | Residue | Details |
| A | VAL134-VAL146 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by RIPK3 and autocatalysis","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29440439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31827280","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
