6OKO
Crystal structure of mRIPK3 complexed with N-(3-fluoro-4-{1H-pyrrolo[2,3-b]pyridin-4-yloxy}phenyl)-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue 1FN A 4000 |
| Chain | Residue |
| A | VAL36 |
| A | LEU132 |
| A | HIS141 |
| A | LEU150 |
| A | LEU159 |
| A | ALA160 |
| A | ASP161 |
| A | PHE162 |
| A | ALA49 |
| A | LYS51 |
| A | GLU61 |
| A | MET65 |
| A | THR95 |
| A | ARG96 |
| A | PHE97 |
| A | MET98 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 1FN B 4000 |
| Chain | Residue |
| B | VAL36 |
| B | ALA49 |
| B | LYS51 |
| B | GLU61 |
| B | LEU68 |
| B | THR95 |
| B | ARG96 |
| B | PHE97 |
| B | MET98 |
| B | LEU132 |
| B | HIS141 |
| B | LEU150 |
| B | LEU159 |
| B | ALA160 |
| B | ASP161 |
| B | PHE162 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGGFGVVFrAhhrtwnhd..........VAVK |
| Chain | Residue | Details |
| A | VAL28-LYS51 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LlHrDLKpsNILL |
| Chain | Residue | Details |
| A | LEU139-LEU151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10490590","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24095729","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24095729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4M69","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24095729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4M69","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Y572","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q9Y572","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23612963","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23612963","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
