Research workbench
Bfl-1 in complex with alpha helical peptide
Analyse Bfl-1 in complex with alpha helical peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RJP
- Type
- protein
- Length
- 334 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-related protein A1; BCL-2-like protein 11
- UniProt
- Q16548, O43521
- Pockets
- 6 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | BCL-2-related protein A1 | protein | 150 | 73% helix, 0% strand | Q16548 |
| C, D | BCL-2-like protein 11 | protein | 17 | 88% helix, 0% strand | O43521 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.51 | 0.79 | 21 | empty |
| 2 | 150 | 0.44 | 0.76 | 19 | empty |
| 3 | 70 | 0.44 | 0.81 | 15 | empty |
| 4 | 129 | 0.39 | 0.74 | 17 | empty |
| 5 | 68 | 0.36 | 0.77 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–C · 891 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 860 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 767 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 1 disulfide (nonstandard, disulfide).
Compared structures
- 6RJP · Bfl-1 in complex with alpha helical peptide · the same entry in another collection · chain D against D, TM-score 1.00
- Q16548 · AlphaFold monomer V2.0 prediction for BCL-2-related protein A1 (Q16548) · a predicted model of the same protein · chain A against A, TM-score 0.95
- O43521 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 11 (O43521) · a predicted model of the same protein · chain D against A, TM-score 0.61
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 Q16548
- Every structure of UniProt O43521
- Elsewhere: RCSB PDB 6RJP · PDBe 6RJP · UniProt Q16548 · UniProt O43521
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