Research workbench
Crystal structure of the first bromodomain of human BRD4 in complex with an acetylated atrx peptide (K1030AC/K1033AC)
Analyse Crystal structure of the first bromodomain of human BRD4 in complex with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G0O
- Type
- protein
- Length
- 136 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60885, P46100
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 125 | — | O60885 |
| B | — | protein | 11 | — | P46100 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G0O · Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated… · the same entry in another collection · chain A against A, TM-score 1.00
- O60885 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 4 (O60885) · a predicted model of the same protein · chain A against A, TM-score 0.97
- P46100 · AlphaFold monomer V2.0 prediction for transcriptional regulator atrx (P46100) · a predicted model of the same protein · chain B against A, TM-score 0.42
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 O60885
- Every structure of UniProt P46100
- Elsewhere: RCSB PDB 6G0O · PDBe 6G0O · UniProt O60885 · UniProt P46100
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