Research workbench
Crystal structure of moz
Analyse Crystal structure of moz in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V43
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT6A; Histone H3.1
- EC
- 2.3.1.48
- UniProt
- Q92794, P68431
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 112 | 13% helix, 9% strand | Q92794 |
| Q | Histone H3.1 | protein | 7 | 0% helix, 29% strand | P68431 |
Ligands and binding sites
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 | 99 | 0.43 | 0.78 | 19 | ACT |
Interfaces
1 interface between chains.
- A–Q · 541 Ų buried · 15 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 Q92794
- Every structure of UniProt P68431
- Elsewhere: RCSB PDB 3V43 · PDBe 3V43 · UniProt Q92794 · UniProt P68431
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