Research workbench
Crystal structure of moz double phd finger mutant-S210D/N235R in complex with histone H3 crotonylation at K14
Analyse Crystal structure of moz double phd finger mutant-S210D/N235R 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
- 5B78
- Type
- protein
- Length
- 141 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT6A; Histone H3
- EC
- 2.3.1.48
- UniProt
- Q92794, K7EMV3
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 119 | 17% helix, 8% strand | Q92794 |
| B | Histone H3 | protein | 22 | 50% helix, 9% strand | K7EMV3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
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 | 58 | 0.42 | 0.82 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1105 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 5B78 · Crystal structure of MOZ double PHD finger mutant-S210D/N235R in complex with histone H3… · 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 0.97
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 K7EMV3
- Elsewhere: RCSB PDB 5B78 · PDBe 5B78 · UniProt Q92794 · UniProt K7EMV3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.