2IVV
Crystal structure of phosphorylated RET tyrosine kinase domain complexed with the inhibitor PP1
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PP1 A3014 |
| Chain | Residue |
| A | LEU730 |
| A | ASP892 |
| A | HOH2123 |
| A | VAL738 |
| A | ALA756 |
| A | LYS758 |
| A | VAL804 |
| A | GLU805 |
| A | ALA807 |
| A | LEU881 |
| A | SER891 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A3012 |
| Chain | Residue |
| A | GLY700 |
| A | PRO701 |
| A | LEU702 |
| A | SER703 |
| A | GLN910 |
| A | LEU923 |
| A | PHE924 |
| A | HIS926 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A3013 |
| Chain | Residue |
| A | ARG873 |
| A | LEU895 |
| A | LYS907 |
| A | GLY911 |
| A | ARG912 |
| A | HOH2122 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGEFGKVVkAtafhlkgragytt.....VAVK |
| Chain | Residue | Details |
| A | LEU730-LYS758 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNILV |
| Chain | Residue | Details |
| A | LEU870-VAL882 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4CKI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20117004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X2M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by caspase-3","evidences":[{"source":"PubMed","id":"21357690","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16928683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16928683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20117004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28846099","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP874 | |
| A | ARG878 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP874 | |
| A | ALA876 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN879 | |
| A | ASP874 | |
| A | ALA876 |
