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Crystal structure of crebbp bromodomain complexd with US13A
Analyse Crystal structure of crebbp bromodomain complexd with US13A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NLK
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-binding protein
- EC
- 2.3.1.48
- UniProt
- Q92793
- Ligands
- 92E
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-binding protein (EC 2.3.1.48) | protein | 115 | 69% helix, 0% strand | Q92793 |
Ligands and binding sites
- 92E · ~{N}-[3-acetamido-5-[(5-ethanoyl-2-ethoxy-phenyl) carbamoyl]phenyl]furan-2-carboxamide · ligand · 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 | 78 | 0.49 | 0.83 | 18 | 92E |
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 5NLK · PDBe 5NLK · UniProt Q92793
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