Research workbench
BCL-xl complex with beclin 1 BH3 domain T108PTHR
Analyse BCL-xl complex with beclin 1 BH3 domain T108PTHR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DCN
- Type
- protein
- Length
- 332 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-xl protein; Beclin-1
- UniProt
- Q07817, Q14457
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | BCL-xl protein | protein | 145 | 71% helix, 0% strand | Q07817 |
| D, C | Beclin-1 | protein | 21 | 86% helix, 0% strand | Q14457 |
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 | 476 | 0.65 | 0.77 | 61 | empty |
| 2 | 72 | 0.39 | 0.78 | 13 | empty |
| 3 | 55 | 0.37 | 0.79 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2248 Ų buried · 33 hydrogen bonds · protein-protein
- A–D · 968 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 930 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6DCN · Bcl-xL complex with Beclin 1 BH3 domain T108pThr · the same entry in another collection · chain C against C, TM-score 1.00
- Q14457 · AlphaFold monomer V2.0 prediction for beclin-1 (Q14457) · a predicted model of the same protein · chain C against A, TM-score 0.78
- 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 0.78
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 Q14457
- Elsewhere: RCSB PDB 6DCN · PDBe 6DCN · UniProt Q07817 · UniProt Q14457
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