Research workbench
Crystal structure of the first bromodomain of human BRD4 in complex with an acetylated POLR2A peptide (K775AC/K778AC)
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
- 6G0R
- Type
- protein
- Length
- 135 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60885, P24928
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 127 | — | O60885 |
| C | — | protein | 8 | — | P24928 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G0R · 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
- P24928 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase II subunit RPB1 (P24928) · a predicted model of the same protein · chain C against A, TM-score 0.53
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 P24928
- Elsewhere: RCSB PDB 6G0R · PDBe 6G0R · UniProt O60885 · UniProt P24928
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