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Crystal structure of pH domain of BRUTON'S tyrosine kinase
Analyse Crystal structure of pH domain of BRUTON'S tyrosine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z0P
- Type
- protein
- Length
- 635 residues
- Chains
- 4
- 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
- 4PT, ZN
- Pockets
- 14 · best druggability 0.46
Structure
x-ray diffraction · 4 distinct chains · 16% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase btk (EC 2.7.10.2) | protein | 158 | 16% helix, 36% strand | Q06187 |
| B | Tyrosine-protein kinase btk (EC 2.7.10.2) | protein | 161 | 15% helix, 35% strand | Q06187 |
| C | Tyrosine-protein kinase btk (EC 2.7.10.2) | protein | 155 | 17% helix, 39% strand | Q06187 |
| D | Tyrosine-protein kinase btk (EC 2.7.10.2) | protein | 161 | 16% helix, 36% strand | Q06187 |
Ligands and binding sites
- 4PT · (2R)-3-{[(S)-{[(2S,3R,5S,6S)-2,6-dihydroxy-3,4,5-tris(phosphonooxy)cyclohexyl]oxy}(hydroxy) phosphoryl]oxy}-2-(1-hydroxybutoxy)propyl butyrate · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.46 | 0.83 | 19 | empty |
| 2 | 84 | 0.45 | 0.81 | 21 | empty |
| 3 | 80 | 0.44 | 0.81 | 20 | empty |
| 4 | 66 | 0.44 | 0.82 | 19 | empty |
| 5 | 72 | 0.40 | 0.79 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1166 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1106 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 567 Ų buried · 5 hydrogen bonds · protein-protein
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 2Z0P · PDBe 2Z0P · UniProt Q06187
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