Research workbench
Crystal structure of the second bromodomain of human BRD2 in complex with the inhibitor Y13158
Analyse Crystal structure of the second bromodomain of human BRD2 in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WNI
- Type
- protein
- Length
- 218 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25440
- Ligands
- JGU
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 110 | — | P25440 |
| B | — | protein | 108 | — | P25440 |
Ligands and binding sites
- JGU · 7-[2-[2,4-bis(fluoranyl)phenoxy]-5-(2-oxidanylpropan-2-yl)phenyl]-2-[4-(2-hydroxyethyloxy)-3,5-dimethyl-phenyl]-5-methyl-furo[3,2-c]pyridin-4-one · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WNI · Crystal Structure of the second bromodomain of human BRD2 in complex with the inhibitor… · the same entry in another collection · chain A against A, TM-score 1.00
- P25440 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 2 (P25440) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 7WNI · PDBe 7WNI · UniProt P25440
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