MolNFT v1 · #153204 · protein
Co-crystal structure of btk kinase domain with zanubrutinib
6J6M · Tyrosine-protein kinase btk: “Co-crystal structure of btk kinase domain with zanubrutinib”. X-ray diffraction, 1 ligand (BA0), 2 pockets (best druggability 0.74). MolNFT v1 #153204 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6J6M
- Type
- protein
- Length
- 267 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
- BA0
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase btk (EC 2.7.10.2) | protein | 267 | 43% helix, 18% strand | Q06187 |
Ligands and binding sites
- BA0 · (7S)-2-(4-phenoxyphenyl)-7-(1-propanoylpiperidin-4-yl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide · ligand · chains A
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.74 | 0.83 | 64 | BA0 |
| 2 | 106 | 0.42 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 6J6M · PDBe 6J6M · UniProt Q06187
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