Crystal structure of human histone acetytransferas 1 (HAT1) in complex with isobutryl-CoA and K12A mutant variant of histone H4

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 28% strand (DSSP).

Ligands and binding sites

• CO6 · Isobutyryl-coenzyme A · ligand · 2 copies · chains A, B
• UNX · Unknown atom or ion · ion · 16 copies · chains A, B
• SO4 · Sulfate ion · ion · 2 copies · chains A, B
• GOL · Glycerol · additive · 3 copies · chains A, C, B
• ACT · Acetate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• B–D · 730 Ų buried · 24 hydrogen bonds · protein-protein
• A–C · 722 Ų buried · 24 hydrogen bonds · protein-protein
• A–B · 390 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (alkylation).

Compared structures

• 6VO5 · Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA… · the same entry in another collection · chain D against D, TM-score 1.00
• O14929 · AlphaFold monomer V2.0 prediction for histone acetyltransferase type B catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 1.00
• P62805 · AlphaFold monomer V2.0 prediction for histone H4 (P62805) · a predicted model of the same protein · chain D against A, TM-score 0.26

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 O14929
• Every structure of UniProt P62805
• Elsewhere: RCSB PDB 6VO5 · PDBe 6VO5 · UniProt O14929 · UniProt P62805