Structural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamily

Keyphrases

• Accession number 10%
• Acyl 30%
• Adenosine Monophosphate 10%
• Aprataxin 10%
• Atomic Coordinates 10%
• Catalytic Specificity 10%
• Class-based 10%
• Endogenous Substrates 10%
• Family Protein 20%
• Fragile Histidine Triad 10%
• Galactose-1-phosphate Uridyltransferase 10%
• High-resolution Crystal Structure 10%
• Histidine 100%
• Histidine Triad nucleotide-binding Protein 1 100%
• Hydrolases 30%
• Nucleotide Hydrolase 20%
• Nucleotide-binding Protein 10%
• Phosphoramidase 30%
• Protein Data Bank 10%
• Protein Enzymes 10%
• Protein Family 30%
• Protein Structure 20%
• Structural Characterization 100%
• Structural Relationship 10%
• Structure-based Phylogeny 10%
• View Interactions 10%
• X-ray Crystallography 10%

Biochemistry, Genetics and Molecular Biology

• Adenosine Monophosphate 38%
• Aprataxin 7%
• Binding Protein 100%
• Cladistics 15%
• Crystal Structure 15%
• Enzyme 30%
• Galactose 1-Phosphate 7%
• Histidine 100%
• Hydrolase 38%
• Protein Data Bank 7%
• Protein Family 23%
• Protein Structure 15%