Research workbench
BCL-xl in a complex with a covalent small molecule inhibitor
Analyse BCL-xl in a complex with a covalent small molecule inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RNU
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-like protein 1
- UniProt
- Q07817
- Ligands
- KBH, BR
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | BCL-2-like protein 1 | protein | 142 | 77% helix, 0% strand | Q07817 |
Ligands and binding sites
- KBH · 4-(4-fluorophenyl)-3-fluorosulfonyl-benzoic acid · ligand · 2 copies · chains A, B
- BR · Bromide ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 620 | 0.79 | 0.85 | 52 | KBH |
| 2 | 70 | 0.33 | 0.75 | 12 | empty |
| 3 | 80 | 0.31 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 471 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 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 Q07817
- Elsewhere: RCSB PDB 6RNU · PDBe 6RNU · UniProt Q07817
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