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Crystal structure of CBP bromodomain liganded with 9c
Analyse Crystal structure of CBP bromodomain liganded with 9c in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EVJ
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.57
- Source
- Homo sapiens
- Molecule
- CREB-binding protein
- EC
- 2.3.1.48
- UniProt
- Q92793
- Ligands
- JE9, PO4
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · resolution 2.57 · 1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CREB-binding protein (EC 2.3.1.48) | protein | 111 | 65% helix, 0% strand | Q92793 |
Ligands and binding sites
- JE9 · 3-acetyl-1-((3-(1-cyclopropyl-1H-pyrazol-4-yl)-2-fluoro-5-(hydroxymethyl)phenyl)carbamoyl)indolizin-7-yl dimethylcarbamate · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.43 | 0.81 | 18 | empty |
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 7EVJ · PDBe 7EVJ · UniProt Q92793
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