6NEC
STRUCTURE OF RET PROTEIN TYROSINE KINASE DOMAIN IN COMPLEX WITH NINTEDANIB
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 |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004713 | molecular_function | protein tyrosine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue XIN A 1101 |
Chain | Residue |
A | GLY731 |
A | ALA807 |
A | LYS808 |
A | GLY810 |
A | LEU881 |
A | ASP892 |
A | ALA756 |
A | LYS758 |
A | GLU775 |
A | LEU779 |
A | ILE788 |
A | VAL804 |
A | GLU805 |
A | TYR806 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue FMT A 1102 |
Chain | Residue |
A | ARG873 |
A | LEU895 |
A | ARG897 |
A | LYS907 |
A | GLY911 |
A | ARG912 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue FMT C 1101 |
Chain | Residue |
A | GLN910 |
A | LEU923 |
A | PHE924 |
A | HIS926 |
C | GLY700 |
C | PRO701 |
C | LEU702 |
C | SER703 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue XIN C 1102 |
Chain | Residue |
C | THR729 |
C | LEU730 |
C | GLY731 |
C | VAL738 |
C | ALA756 |
C | LYS758 |
C | GLU775 |
C | LEU779 |
C | ILE788 |
C | VAL804 |
C | GLU805 |
C | TYR806 |
C | ALA807 |
C | LYS808 |
C | TYR809 |
C | GLY810 |
C | LEU881 |
C | SER891 |
C | ASP892 |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
Chain | Residue | Details |
A | ASP874 | |
C | ASP874 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924, ECO:0007744|PDB:4CKI |
Chain | Residue | Details |
A | LEU730 | |
C | LEU730 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:24560924 |
Chain | Residue | Details |
A | LYS758 | |
C | LYS758 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20117004, ECO:0007744|PDB:2X2M |
Chain | Residue | Details |
A | GLU805 | |
C | GLU805 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:21357690 |
Chain | Residue | Details |
A | ASP707 | |
C | ASP707 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
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 | |
C | LEU712 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813 |
Chain | Residue | Details |
A | TYR806 | |
A | TYR809 | |
C | TYR806 | |
C | TYR809 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24560924 |
Chain | Residue | Details |
A | TYR826 | |
C | TYR826 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:24560924 |
Chain | Residue | Details |
A | TYR900 | |
C | TYR900 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
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 | TYR905 | |
C | TYR905 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:24560924 |
Chain | Residue | Details |
A | TYR981 | |
C | TYR981 |