4ITH
Crystal structure of RIP1 kinase in complex with necrostatin-1 analog
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 301 |
| Chain | Residue |
| A | ILE232 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD A 304 |
| Chain | Residue |
| A | ARG286 |
| A | HOH424 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 305 |
| Chain | Residue |
| A | ARG258 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RCM A 307 |
| Chain | Residue |
| A | LEU129 |
| A | HIS136 |
| A | ILE154 |
| A | ALA155 |
| A | ASP156 |
| A | SER161 |
| A | PHE162 |
| A | MET67 |
| A | VAL75 |
| A | VAL76 |
| A | LEU78 |
| A | MET92 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 301 |
| Chain | Residue |
| B | HIS56 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 303 |
| Chain | Residue |
| B | ARG286 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 305 |
| Chain | Residue |
| B | TRP268 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RCM B 307 |
| Chain | Residue |
| B | MET67 |
| B | LEU70 |
| B | VAL75 |
| B | VAL76 |
| B | LEU78 |
| B | MET92 |
| B | ILE154 |
| B | ALA155 |
| B | ASP156 |
| B | SER161 |
| B | 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 | 2 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by RIPK3 and autocatalysis","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
