Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation

Medicine & Life Sciences

• N-Terminal Acetyltransferases 100%
• Acetylation 56%
• Methionine 55%
• Transferases 27%
• Lysine Acetyltransferases 23%
• Enzymes 22%
• N-acetyltalosaminuronic acid 21%
• Peptide Fragments 17%
• Histone Acetyltransferases 17%
• Acetyltransferases 17%
• Peptides 17%
• Chromatids 16%
• Coenzyme A 16%
• Hydrogen Bonding 16%
• Histidine 14%
• Eukaryota 13%
• Mutagenesis 13%
• Lysine 13%
• Tyrosine 12%
• Chromosomes 10%
• X-Rays 10%
• Proteins 9%
• Therapeutics 4%
• Neoplasms 4%

Chemical Compounds

• Methionine Residue 71%
• Acetylation 54%
• Lysine 50%
• Molecular Scaffold 33%
• Cohesion 32%
• Peptide 31%
• Tyrosine Residue 30%
• Histidine Residue 30%
• Histone 28%
• Protein 22%
• Condensation 19%
• Hydrogen Bond 16%
• Modification 14%
• Crystal Structure 13%
• Molecule 9%
• Application 8%