Crystal structure of the natc complex bound to gag peptide and CoA

Structure

x-ray diffraction · 4 distinct chains · 54% helix, 13% strand (DSSP).

Ligands and binding sites

• COA · Coenzyme A · ligand · chains A, D
• IOD · Iodide ion · ion · 10 copies · chains A, B, C
• CL · Chloride ion · ion · 6 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 5 copies · chains B

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

Pockets

14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• B–C · 2055 Ų buried · 34 hydrogen bonds · protein-protein
• A–B · 1907 Ų buried · 18 hydrogen bonds · protein-protein
• A–D · 455 Ų buried · 8 hydrogen bonds · protein-protein
• A–C · 314 Ų buried · 4 hydrogen bonds · protein-protein
• B–D · 211 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 6YGD · Crystal structure of the NatC complex bound to Gag peptide and CoA · the same entry in another collection · chain A against A, TM-score 1.00
• Q03503 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 30 (Q03503) · a predicted model of the same protein · chain A against A, TM-score 0.98
• P23059 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 38, natc auxiliary… · a predicted model of the same protein · chain C against A, TM-score 0.98
• Q02197 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 35, natc auxiliary… · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q03503
• Every structure of UniProt Q02197
• Every structure of UniProt P23059
• Every structure of UniProt P32503
• Elsewhere: RCSB PDB 6YGD · PDBe 6YGD · UniProt Q03503 · UniProt Q02197 · UniProt P23059 · UniProt P32503