MolNFT v1 · #75192 · protein
Crystal structure of btk kinase domain complexed with 2-isopropyl-7- (4-methyl-piperazin-1-yl)-4-(5-methyl-2H-pyrazol-3-ylamino)-2H- phthalazin-1-one
3PIX · Tyrosine-protein kinase btk: “Crystal structure of btk kinase domain complexed with 2-isopropyl-7…”. X-ray diffraction, 1 ligand (027), 4 pockets (best druggability 0.53). MolNFT v1 #75192 on GenesisL1: 3D structure, binding sites…
- PDB
- 3PIX
- Type
- protein
- Length
- 268 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
- 027
- Pockets
- 4 · best druggability 0.53
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 | 268 | 44% helix, 17% strand | Q06187 |
Ligands and binding sites
- 027 · 7-(4-methylpiperazin-1-yl)-4-[(5-methyl-1H-pyrazol-3-yl)amino]-2-(propan-2-yl)phthalazin-1(2H)-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.53 | 0.78 | 25 | 027 |
| 2 | 106 | 0.52 | 0.82 | 25 | empty |
| 3 | 69 | 0.37 | 0.78 | 15 | empty |
| 4 | 69 | 0.37 | 0.78 | 19 | empty |
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 3PIX · PDBe 3PIX · UniProt Q06187
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