8PQE
c-KIT kinase domain in complex with avapritinib derivative 11
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 | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
Functional Information from PROSITE/UniProt
site_id | PS00024 |
Number of Residues | 16 |
Details | HEMOPEXIN Hemopexin domain signature. LPvkWmapEsIFNSVY |
Chain | Residue | Details |
A | LEU831-TYR846 |
site_id | PS00107 |
Number of Residues | 29 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaqgliksdaamt.....VAVK |
Chain | Residue | Details |
A | LEU595-LYS623 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL |
Chain | Residue | Details |
A | CYS788-LEU800 |
site_id | PS00240 |
Number of Residues | 14 |
Details | RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHeNIVNLLGACT |
Chain | Residue | Details |
A | GLY648-THR661 |
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 | ASP792 | |
B | ASP792 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | TYR568 | |
B | LYS623 | |
B | GLU671 | |
B | ARG796 | |
B | ASN797 | |
B | ASP810 | |
A | GLY596 | |
A | LYS623 | |
A | GLU671 | |
A | ARG796 | |
A | ASN797 | |
A | ASP810 | |
B | TYR568 | |
B | GLY596 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:20147452 |
Chain | Residue | Details |
A | TYR553 | |
B | TYR553 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210 |
Chain | Residue | Details |
A | TYR568 | |
B | TYR568 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210 |
Chain | Residue | Details |
A | TYR570 | |
B | TYR570 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802 |
Chain | Residue | Details |
A | SER821 | |
B | SER821 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452 |
Chain | Residue | Details |
A | TYR823 | |
B | TYR823 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163 |
Chain | Residue | Details |
A | SER891 | |
B | SER891 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452 |
Chain | Residue | Details |
A | TYR900 | |
B | TYR900 |