6NJA
Structure of WT RET protein tyrosine kinase domain at 1.92A resolution.
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue ADE A 1101 |
| Chain | Residue |
| A | LEU730 |
| A | VAL738 |
| A | ALA756 |
| A | GLU805 |
| A | TYR806 |
| A | ALA807 |
| A | LEU881 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue FMT A 1102 |
| Chain | Residue |
| A | LEU702 |
| A | SER703 |
| A | GLN910 |
| A | LEU923 |
| A | PHE924 |
| A | HIS926 |
| A | GLY700 |
| A | PRO701 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 1103 |
| Chain | Residue |
| A | ARG873 |
| A | LEU895 |
| A | GLY911 |
| A | ARG912 |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| A | ASP874 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924, ECO:0007744|PDB:4CKI |
| Chain | Residue | Details |
| A | LEU730 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924 |
| Chain | Residue | Details |
| A | LYS758 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20117004, ECO:0007744|PDB:2X2M |
| Chain | Residue | Details |
| A | GLU805 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:21357690 |
| Chain | Residue | Details |
| A | ASP707 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Breakpoint for translocation to form PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-TRIM24 and RET-TRIM33 oncogenes => ECO:0000269|PubMed:10439047, ECO:0000269|PubMed:10980597, ECO:0000269|PubMed:2406025, ECO:0000269|PubMed:2734021 |
| Chain | Residue | Details |
| A | LEU712 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813 |
| Chain | Residue | Details |
| A | TYR809 | |
| A | TYR806 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24560924 |
| Chain | Residue | Details |
| A | TYR826 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:24560924 |
| Chain | Residue | Details |
| A | PTR900 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:20117004, ECO:0000269|PubMed:24560924, ECO:0000269|PubMed:28846099 |
| Chain | Residue | Details |
| A | PTR905 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:24560924 |
| Chain | Residue | Details |
| A | TYR981 |
