5AMN
The Discovery of 2-Substituted Phenol Quinazolines as Potent and Selective RET Kinase Inhibitors
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FMT A 2011 |
Chain | Residue |
A | GLY700 |
A | PRO701 |
A | LEU702 |
A | SER703 |
A | GLN910 |
A | LEU923 |
A | PHE924 |
A | HIS926 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 2012 |
Chain | Residue |
A | LEU895 |
A | LYS907 |
A | GLY911 |
A | ARG912 |
A | ARG873 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 2013 |
Chain | Residue |
A | ASP707 |
A | LYS728 |
A | LYS740 |
A | TYR806 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 2014 |
Chain | Residue |
A | HOH3039 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 2015 |
Chain | Residue |
A | ALA866 |
A | VAL997 |
A | PHE998 |
A | ALA999 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 2016 |
Chain | Residue |
A | LYS747 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 2017 |
Chain | Residue |
A | THR754 |
A | PHE924 |
A | HOH3009 |
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 | TYR806 | |
A | TYR809 |
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 |