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Crystal structure of btk kinase domain complexed with (5-amino-1-O- tolyl-1H-pyrazol-4-yl)-[3-(1-methanesulfonyl-piperidin-4-yl)-phenyl]- methanone
Analyse Crystal structure of btk kinase domain complexed with (5-amino-1-O… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PIZ
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase btk
- EC
- 2.7.10.2
- UniProt
- Q06187
- Ligands
- 03C
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase btk (EC 2.7.10.2) | protein | 245 | 44% helix, 17% strand | Q06187 |
Ligands and binding sites
- 03C · [5-amino-1-(2-methylphenyl)-1H-pyrazol-4-yl]{3-[1-(methylsulfonyl)piperidin-4-yl]phenyl}methanone · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.58 | 0.80 | 25 | 03C |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q06187
- Elsewhere: RCSB PDB 3PIZ · PDBe 3PIZ · UniProt Q06187
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