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Crystal structure of cbp bromodomain liganded with Y08284
Analyse Crystal structure of cbp bromodomain liganded with Y08284 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XNE
- Type
- protein
- Length
- 230 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
- GHF
- Pockets
- 1 · best druggability 0.78
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 | 115 | 68% helix, 0% strand | Q92793 |
Ligands and binding sites
- GHF · N-[3-(1-cyclopropylpyrazol-4-yl)-2-fluoranyl-5-[(1S)-1-oxidanylethyl]phenyl]-3-ethanoyl-7-methoxy-indolizine-1-carboxamide · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 736 | 0.78 | 0.82 | 52 | GHF |
Interfaces
1 interface between chains.
- A–B · 388 Ų buried · 5 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 7XNE · PDBe 7XNE · UniProt Q92793
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