6NW2
Structure of human RIPK1 kinase domain in complex with compound 11
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue L4Y A 301 |
Chain | Residue |
A | ILE43 |
A | LEU157 |
A | LEU159 |
A | HOH473 |
A | LYS45 |
A | MET67 |
A | VAL75 |
A | VAL76 |
A | LEU78 |
A | LEU90 |
A | MET92 |
A | ASP156 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue L4Y B 301 |
Chain | Residue |
B | VAL31 |
B | ILE43 |
B | LYS45 |
B | MET67 |
B | VAL75 |
B | VAL76 |
B | LEU78 |
B | LEU90 |
B | MET92 |
B | ILE154 |
B | ASP156 |
B | LEU157 |
B | LEU159 |
B | HOH424 |
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 |