6I82
Crystal structure of partially phosphorylated RET V804M tyrosine kinase domain complexed with PDD00018412
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue H6W A 1101 |
| Chain | Residue |
| A | LEU730 |
| A | ASP892 |
| A | FMT1110 |
| A | HOH1246 |
| A | PHE735 |
| A | ALA756 |
| A | GLU805 |
| A | ALA807 |
| A | GLY810 |
| A | ARG878 |
| A | ASN879 |
| A | LEU881 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 1102 |
| Chain | Residue |
| A | LEU846 |
| A | FMT1111 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 1103 |
| Chain | Residue |
| A | ARG969 |
| A | GLU971 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue FMT A 1104 |
| Chain | Residue |
| A | GLY700 |
| A | PRO701 |
| A | LEU702 |
| A | SER703 |
| B | GLN910 |
| B | LEU923 |
| B | PHE924 |
| B | HIS926 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 1105 |
| Chain | Residue |
| A | SER703 |
| A | LEU704 |
| A | HOH1209 |
| A | HOH1262 |
| B | LYS740 |
| B | EDO1105 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 1106 |
| Chain | Residue |
| A | THR742 |
| A | TYR752 |
| A | HOH1267 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 1107 |
| Chain | Residue |
| A | ALA866 |
| A | VAL997 |
| A | PHE998 |
| A | ALA999 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 1108 |
| Chain | Residue |
| A | ASN723 |
| A | TYR752 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 1109 |
| Chain | Residue |
| A | SER705 |
| A | ARG770 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 1110 |
| Chain | Residue |
| A | GLU775 |
| A | SER891 |
| A | ASP892 |
| A | PHE893 |
| A | H6W1101 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 1111 |
| Chain | Residue |
| A | SER819 |
| A | ARG844 |
| A | ALA845 |
| A | LEU846 |
| A | LEU947 |
| A | EDO1102 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 1101 |
| Chain | Residue |
| B | GLU775 |
| B | MET804 |
| B | ASP892 |
| B | H6W1102 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue H6W B 1102 |
| Chain | Residue |
| B | LEU730 |
| B | PHE735 |
| B | VAL738 |
| B | ALA756 |
| B | GLU805 |
| B | ALA807 |
| B | ARG878 |
| B | ASN879 |
| B | LEU881 |
| B | ASP892 |
| B | CL1101 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 1103 |
| Chain | Residue |
| B | ARG721 |
| B | CYS794 |
| B | GLN796 |
| B | ASP797 |
| B | GLY798 |
| B | PRO799 |
| B | LEU801 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1104 |
| Chain | Residue |
| B | ASP898 |
| B | VAL899 |
| B | TYR900 |
| B | GLU901 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 1105 |
| Chain | Residue |
| A | FMT1105 |
| B | THR754 |
| B | PHE924 |
| B | ASP925 |
| B | FMT1111 |
| B | HOH1263 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue FMT B 1106 |
| Chain | Residue |
| B | ARG721 |
| B | LEU726 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue FMT B 1107 |
| Chain | Residue |
| B | ARG873 |
| B | LEU895 |
| B | ARG897 |
| B | LYS907 |
| B | GLY911 |
| B | ARG912 |
| B | ILE913 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 1108 |
| Chain | Residue |
| B | THR930 |
| B | GLN931 |
| B | VAL997 |
| B | PHE998 |
| B | HOH1285 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 1109 |
| Chain | Residue |
| B | MET1008 |
| B | ARG1012 |
| B | HOH1202 |
| B | SER977 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 1110 |
| Chain | Residue |
| B | LYS728 |
| B | LEU730 |
| B | LYS740 |
| B | TYR806 |
| B | HOH1204 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue FMT B 1111 |
| Chain | Residue |
| B | ILE920 |
| B | ASP925 |
| B | EDO1105 |
| site_id | AE5 |
| Number of Residues | 2 |
| Details | binding site for residue FMT B 1112 |
| Chain | Residue |
| B | HIS784 |
| B | GLN860 |
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 | 2 |
| 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 | 16 |
| 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 | 2 |
| 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 | 4 |
| 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 | 1 |
| Details | Site: {"description":"Breakpoint for translocation to form PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-TRIM24 and RET-TRIM33 oncogenes","evidences":[{"source":"PubMed","id":"10439047","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10980597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2406025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2734021","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14711813","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| 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_FI9 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"24560924","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| 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 |
