Research workbench
Human myst histone acetyltransferase 1
Analyse Human myst histone acetyltransferase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WCI
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT8
- EC
- 2.3.1.48
- UniProt
- Q9H7Z6
- Ligands
- 1VU, ZN, CL
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT8 (EC 2.3.1.48) | protein | 284 | 33% helix, 23% strand | Q9H7Z6 |
Ligands and binding sites
- 1VU · propionyl Coenzyme A · ligand · chains A
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.70 | 0.83 | 37 | 1VU |
| 2 | 73 | 0.42 | 0.80 | 19 | empty |
| 3 | 74 | 0.34 | 0.76 | 19 | EDO |
Modifications
Observed in the structure: 1 modified (acetylation).
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 Q9H7Z6
- Elsewhere: RCSB PDB 5WCI · PDBe 5WCI · UniProt Q9H7Z6
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