Research workbench
Crystal structure of a pro-survival BCL-2:BIM BH3 complex
Analyse Crystal structure of a pro-survival BCL-2:BIM BH3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B4S
- Type
- protein
- Length
- 172 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-like protein 10; BCL-2-like protein 11
- UniProt
- Q9HD36, O43521
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-like protein 10 | protein | 148 | 71% helix, 0% strand | Q9HD36 |
| B | BCL-2-like protein 11 | protein | 24 | 83% helix, 0% strand | O43521 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 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 | 55 | 0.29 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1020 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4B4S · Crystal Structure of a pro-survival Bcl-2:Bim BH3 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HD36 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 10 (Q9HD36) · a predicted model of the same protein · chain A against A, TM-score 0.98
- 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 0.70
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 Q9HD36
- Every structure of UniProt O43521
- Elsewhere: RCSB PDB 4B4S · PDBe 4B4S · UniProt Q9HD36 · UniProt O43521
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