Crystal structure of GCN5-related N-acetyltransferase from kribbella flavida

Structure

x-ray diffraction · 3 distinct chains · 35% helix, 32% strand (DSSP).

Ligands and binding sites

• ACO · Acetyl coenzyme *A · ligand · 5 copies · chains A, B, E, D, C, F
• AC8 · [(2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-bis(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl dihydrogen diphosphate · ligand · chains A, C, D
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 6 copies · chains A, B, C, D, E, F
• GOL · Glycerol · additive · 2 copies · chains A, C, E

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Interfaces

12 interfaces between chains.

• A–B · 2124 Ų buried · 23 hydrogen bonds · protein-protein
• C–D · 2121 Ų buried · 20 hydrogen bonds · protein-protein
• E–F · 2062 Ų buried · 21 hydrogen bonds · protein-protein
• A–C · 810 Ų buried · 9 hydrogen bonds · protein-protein
• B–D · 759 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 30 modified (engineered).

Compared structures

• 4MY0 · Crystal Structure of GCN5-related N-acetyltransferase from Kribbella flavida · the same entry in another collection · chain A against A, TM-score 1.00

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 D2PVF8
• Elsewhere: RCSB PDB 4MY0 · PDBe 4MY0 · UniProt D2PVF8