6NYH
Structure of human RIPK1 kinase domain in complex with GNE684
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 15 | 
| Details | binding site for residue L8D A 301 | 
| Chain | Residue | 
| A | ILE43 | 
| A | HIS136 | 
| A | ILE154 | 
| A | ASP156 | 
| A | LEU157 | 
| A | LEU159 | 
| A | HOH481 | 
| A | LYS45 | 
| A | MET67 | 
| A | VAL75 | 
| A | VAL76 | 
| A | LEU78 | 
| A | LEU90 | 
| A | MET92 | 
| A | LEU129 | 
| site_id | AC2 | 
| Number of Residues | 1 | 
| Details | binding site for residue IOD A 303 | 
| Chain | Residue | 
| A | HOH458 | 
| site_id | AC3 | 
| Number of Residues | 15 | 
| Details | binding site for residue L8D B 301 | 
| Chain | Residue | 
| B | ILE43 | 
| B | LYS45 | 
| B | MET67 | 
| B | VAL75 | 
| B | VAL76 | 
| B | LEU78 | 
| B | LEU90 | 
| B | MET92 | 
| B | LEU129 | 
| B | HIS136 | 
| B | ILE154 | 
| B | ASP156 | 
| B | LEU157 | 
| B | LEU159 | 
| B | HOH447 | 
| site_id | AC4 | 
| Number of Residues | 1 | 
| Details | binding site for residue IOD B 302 | 
| Chain | Residue | 
| B | ILE232 | 
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 | 






