MolNFT v1 · #64870 · protein
Crystal structure of the bromodomain of human pcaf
3GG3 · Histone acetyltransferase pcaf: “Crystal structure of the bromodomain of human pcaf”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.59). MolNFT v1 #64870 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3GG3
- Type
- protein
- Length
- 211 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase pcaf
- EC
- 2.3.1.48
- UniProt
- Q92831
- Ligands
- CL
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase pcaf (EC 2.3.1.48) | protein | 107 | 66% helix, 0% strand | Q92831 |
| B | Histone acetyltransferase pcaf (EC 2.3.1.48) | protein | 104 | 69% helix, 0% strand | Q92831 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.59 | 0.84 | 21 | empty |
| 2 | 287 | 0.56 | 0.76 | 33 | empty |
| 3 | 105 | 0.51 | 0.81 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 747 Ų buried · 11 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 Q92831
- Elsewhere: RCSB PDB 3GG3 · PDBe 3GG3 · UniProt Q92831
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