Research workbench
Crystal structure of anti-apoptotic BHRF1 in complex with the bim BH3 domain
Analyse Crystal structure of anti-apoptotic BHRF1 in complex with the bim BH3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WH6
- Type
- protein
- Length
- 179 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Early antigen protein R; BCL-2-like protein 11
- UniProt
- P03182, O43521
- Ligands
- BR
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Early antigen protein R | protein | 157 | 76% helix, 0% strand | P03182 |
| B | BCL-2-like protein 11 | protein | 22 | 77% helix, 0% strand | O43521 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1046 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2WH6 · Crystal structure of anti-apoptotic BHRF1 in complex with the Bim BH3 domain · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.72
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 P03182
- Every structure of UniProt O43521
- Elsewhere: RCSB PDB 2WH6 · PDBe 2WH6 · UniProt P03182 · UniProt O43521
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