Research workbench
Crystal structure of BMX non-receptor tyrosine kinase complexed with PP2
Analyse Crystal structure of BMX non-receptor tyrosine kinase complexed with PP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SXS
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.89
- Source
- Homo sapiens
- Molecule
- Cytoplasmic tyrosine-protein kinase BMX
- EC
- 2.7.10.2
- UniProt
- P51813
- Ligands
- PP2
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · resolution 1.89 · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic tyrosine-protein kinase BMX (EC 2.7.10.2) | protein | 264 | 40% helix, 23% strand | P51813 |
Ligands and binding sites
- PP2 · 1-tert-butyl-3-(4-chloro-phenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.65 | 0.83 | 31 | PP2 |
| 2 | 76 | 0.50 | 0.84 | 21 | empty |
| 3 | 68 | 0.34 | 0.76 | 18 | empty |
Compared structures
- 3SXS · Crystal structure of bmx non-receptor tyrosine kinase complexed with PP2 · the same entry in another collection · chain A against A, TM-score 1.00
- P51813 · AlphaFold monomer V2.0 prediction for cytoplasmic tyrosine-protein kinase bmx (P51813) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P51813
- Elsewhere: RCSB PDB 3SXS · PDBe 3SXS · UniProt P51813
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