Research workbench
Crystal structrue of moz double phd finger in complex with histone H3 propionylation at K14
Analyse Crystal structrue of moz double phd finger in complex with histone H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B77
- 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, SO4
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 116 | 16% helix, 9% strand | Q92794 |
| B | Histone H3 | protein | 25 | 64% helix, 8% strand | K7EMV3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1138 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 5B77 · Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at… · 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 0.98
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 5B77 · PDBe 5B77 · UniProt Q92794 · UniProt K7EMV3
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