8S9F
Crystal structure of the kinase domain of Bruton's Tyrosine Kinase bound to dasatinib
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 PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 23 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGQFGVVKyGkwrgqyd...........VAIK |
| Chain | Residue | Details |
| B | LEU408-LYS430 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV |
| Chain | Residue | Details |
| B | PHE517-VAL529 |
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 |
| B | ASP521 | |
| A | ASP521 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| B | LEU408 | |
| B | LYS430 | |
| A | LEU408 | |
| A | LYS430 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8629002, ECO:0007744|PubMed:17947660 |
| Chain | Residue | Details |
| B | GLU551 | |
| A | GLU551 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q06187 |
| Chain | Residue | Details |
| B | SER604 | |
| B | SER623 | |
| B | SER659 | |
| A | SER604 | |
| A | SER623 | |
| A | SER659 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q06187 |
| Chain | Residue | Details |
| B | PRO617 | |
| A | PRO617 |
