Research workbench
Crystal structure of human myst histone acetyltransferase 3 in complex with acetylcoenzyme a
Analyse Crystal structure of human myst histone acetyltransferase 3 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OZU
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase MYST3
- EC
- 2.3.1.48
- UniProt
- Q92794
- Ligands
- ACM, ACO, ZN
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase MYST3 (EC 2.3.1.48) | protein | 254 | 36% helix, 24% strand | Q92794 |
Ligands and binding sites
- ACM · Acetamide · ligand · 4 copies · chains A
- ACO · Acetyl coenzyme *A · ligand · chains A
- ZN · Zinc ion · metal · 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 | 475 | 0.69 | 0.80 | 51 | ACO, ACM |
| 2 | 137 | 0.42 | 0.75 | 17 | empty |
| 3 | 62 | 0.31 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 4 covalent, 1 modified (covalent ligand, acetylation).
Compared structures
- 2OZU · Crystal structure of human MYST histone acetyltransferase 3 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT6A (Q92794) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q92794
- Elsewhere: RCSB PDB 2OZU · PDBe 2OZU · UniProt Q92794
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