MolNFT v1 · #149120 · protein
Crystal structure of crebbp bromodomain complexd with DR46
6FQT · Creb-binding protein: “Crystal structure of crebbp bromodomain complexd with DR46”. X-ray diffraction, 1 ligand (AY2), 1 pocket (best druggability 0.47). MolNFT v1 #149120 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6FQT
- Type
- protein
- Length
- 114 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
- AY2
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-binding protein (EC 2.3.1.48) | protein | 114 | 67% helix, 0% strand | Q92793 |
Ligands and binding sites
- AY2 · ~{N}-[3-(5-ethanoyl-2-ethoxy-phenyl)-5-(1-methylpyrazol-3-yl)phenyl]furan-2-carboxamide · ligand · 2 copies · 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 | 79 | 0.47 | 0.82 | 20 | AY2 |
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 6FQT · PDBe 6FQT · UniProt Q92793
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