Research workbench
Solution structure of BCL-xl in complex with puma BH3 peptide
Analyse Solution structure of BCL-xl in complex with puma BH3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M04
- Type
- protein
- Length
- 199 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-like protein 1; BCL-2-binding component 3
- UniProt
- Q07817, Q9BXH1
- Pockets
- 6 · best druggability 0.78
Structure
solution nmr · 2 distinct chains · 60% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-like protein 1 | protein | 174 | 59% helix, 0% strand | Q07817 |
| B | BCL-2-binding component 3 | protein | 25 | 68% helix, 0% strand | Q9BXH1 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.78 | 0.96 | 23 | empty |
| 2 | 53 | 0.69 | 0.96 | 21 | empty |
| 3 | 113 | 0.49 | 0.80 | 24 | empty |
| 4 | 70 | 0.48 | 0.83 | 17 | empty |
| 5 | 67 | 0.33 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1546 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2M04 · Solution structure of BCL-xL in complex with PUMA BH3 peptide · 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 0.66
- Q9BXH1 · AlphaFold monomer V2.0 prediction for BCL-2-binding component 3, isoforms 1/2 (Q9BXH1) · a predicted model of the same protein · chain B against A, TM-score 0.45
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 Q9BXH1
- Elsewhere: RCSB PDB 2M04 · PDBe 2M04 · UniProt Q07817 · UniProt Q9BXH1
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