4RG0
Crystal structure of BTK kinase domain complexed with 2-[8-fluoro-2-[2-(hydroxymethyl)-3-[1-methyl-5-[[5-(4-methylpiperazin-1-yl)-2-pyridyl]amino]-6-oxo-3-pyridyl]phenyl]-1-oxo-3,4-dihydroisoquinolin-6-yl]-2-methyl-propanenitrile
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE 3P0 A 701 |
Chain | Residue |
A | GLY411 |
A | ALA478 |
A | GLY480 |
A | HIS519 |
A | ASP521 |
A | ASN526 |
A | SER538 |
A | ASP539 |
A | HOH1027 |
A | HOH1051 |
A | HOH1073 |
A | PHE413 |
A | VAL416 |
A | ALA428 |
A | LYS430 |
A | THR474 |
A | GLU475 |
A | TYR476 |
A | MET477 |
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 |
A | LEU408-LYS430 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV |
Chain | Residue | Details |
A | PHE517-VAL529 |
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 | ASP521 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU408 | |
A | LYS430 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT |
Chain | Residue | Details |
A | THR474 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY |
Chain | Residue | Details |
A | LEU542 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831 |
Chain | Residue | Details |
A | TYR551 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER604 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15375214 |
Chain | Residue | Details |
A | TYR617 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15375214 |
Chain | Residue | Details |
A | SER623 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | SER659 |