Research workbench
Crystal structure of cbp bromodomain liganded with Y08092(31G)
Analyse Crystal structure of cbp bromodomain liganded with Y08092(31G) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XNG
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-binding protein
- EC
- 2.3.1.48
- UniProt
- Q92793
- Ligands
- GI5
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Creb-binding protein (EC 2.3.1.48) | protein | 113 | 68% helix, 0% strand | Q92793 |
Ligands and binding sites
- GI5 · 3-[(1-ethanoylindol-3-yl)carbonylamino]-5-[[(2S)-oxan-2-yl]oxymethyl]benzoic acid · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · chains B
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.74 | 0.82 | 40 | PEG, GI5 |
| 2 | 83 | 0.50 | 0.82 | 17 | GI5 |
Interfaces
1 interface between chains.
- A–B · 477 Ų buried · 7 hydrogen bonds · protein-protein
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 Q92793
- Elsewhere: RCSB PDB 7XNG · PDBe 7XNG · UniProt Q92793
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.