Research workbench
Crystal structure of CREBBP-Y1503C histone acetyltransferase domain in complex with Coenzyme A
Analyse Crystal structure of CREBBP-Y1503C histone acetyltransferase domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8CNB
- Type
- protein
- Length
- 531 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.986
- Source
- Mus musculus
- Molecule
- histone acetyltransferase
- EC
- 2.3.1.48
- UniProt
- F8VPR5
- Ligands
- COA, ZN
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · resolution 1.986 · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | histone acetyltransferase (EC 2.3.1.48) | protein | 531 | 39% helix, 16% strand | F8VPR5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.74 | 0.83 | 48 | COA |
| 2 | 243 | 0.69 | 0.85 | 43 | empty |
| 3 | 348 | 0.59 | 0.77 | 39 | empty |
| 4 | 265 | 0.57 | 0.77 | 44 | empty |
| 5 | 96 | 0.50 | 0.82 | 19 | empty |
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
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 F8VPR5
- Elsewhere: RCSB PDB 8CNB · PDBe 8CNB · UniProt F8VPR5
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