Research workbench
Crystal structure of moz double phd finger histone H3K9AC complex
Analyse Crystal structure of moz double phd finger histone H3K9AC complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LKA
- Type
- protein
- Length
- 138 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
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 126 | 14% helix, 10% strand | Q92794 |
| B | Histone H3.1 | protein | 12 | 67% helix, 17% strand | P68431 |
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.
Interfaces
1 interface between chains.
- A–B · 698 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 4LKA · Crystal Structure of MOZ double PHD finger histone H3K9ac complex · 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 0.94
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 4LKA · PDBe 4LKA · UniProt Q92794 · UniProt P68431
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