Research workbench
BCL-xl with mouse bak BH3 Q75L complex
Analyse BCL-xl with mouse bak BH3 Q75L complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FMJ
- Type
- protein
- Length
- 177 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-like protein 1; BAK1 protein
- UniProt
- Q07817, Q91WX5
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-like protein 1 | protein | 153 | 80% helix, 0% strand | Q07817 |
| B | BAK1 protein | protein | 24 | 71% helix, 0% strand | Q91WX5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · 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 | 129 | 0.56 | 0.83 | 21 | EDO |
| 2 | 57 | 0.29 | 0.75 | 15 | EDO |
| 3 | 62 | 0.28 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1106 Ų buried · 14 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 Q07817
- Every structure of UniProt Q91WX5
- Elsewhere: RCSB PDB 5FMJ · PDBe 5FMJ · UniProt Q07817 · UniProt Q91WX5
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