Research workbench
BRD2-BD2 in complex with a diacetylated-H2A.Z peptide
Analyse BRD2-BD2 in complex with a diacetylated-H2A.Z peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JX7
- Type
- protein
- Length
- 117 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 2; Diacetylated-H2A.Z peptide
- UniProt
- P25440
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain-containing protein 2 | protein | 111 | 68% helix, 0% strand | P25440 |
| B | Diacetylated-H2A.Z peptide | protein | 6 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 448 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (acetylation).
Compared structures
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 P25440
- Elsewhere: RCSB PDB 7JX7 · PDBe 7JX7 · UniProt P25440
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