MolNFT v1 · #114259 · protein
Crystal structure of moz double phd finger in complex with histone H3 butyrylation at K14
5B75 · Histone acetyltransferase KAT6A: “Crystal structure of moz double phd finger in complex with histone H3 butyrylation at K14”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.61). MolNFT v1 #114259 on…
- PDB
- 5B75
- Type
- protein
- Length
- 144 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
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 119 | 15% helix, 8% 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.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.61 | 0.92 | 18 | empty |
| 2 | 76 | 0.46 | 0.81 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1140 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 5B75 · Crystal structure of MOZ double PHD finger in complex with histone H3 butyrylation at K14 · 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 5B75 · PDBe 5B75 · UniProt Q92794 · UniProt K7EMV3
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