Research workbench
Structure of Bcl-xL bound to BimSAHB
Analyse Structure of Bcl-xL bound to BimSAHB in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YQ6
- Type
- protein
- Length
- 163 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.799
- Source
- HOMO SAPIENS; SYNTHETIC CONSTRUCT
- Molecule
- BCL-2-like protein 1; Bim beta 5
- UniProt
- Q07817, O43521
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · resolution 1.799 · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-like protein 1 | protein | 145 | 80% helix, 0% strand | Q07817 |
| B | Bim beta 5 | protein | 18 | 89% helix, 0% strand | O43521 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.36 | 0.75 | 21 | GOL |
Interfaces
1 interface between chains.
- A–B · 903 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 2YQ6 · Structure of BCL-xl bound to bimsahb · the same entry in another collection · chain A against A, TM-score 1.00
- Q07817 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 1 (Q07817) · a predicted model of the same protein · chain A against A, TM-score 0.78
- O43521 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 11 (O43521) · a predicted model of the same protein · chain B against A, TM-score 0.76
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 Q07817
- Every structure of UniProt O43521
- Elsewhere: RCSB PDB 2YQ6 · PDBe 2YQ6 · UniProt Q07817 · UniProt O43521
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