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Sir2Af2-NAD-ADPribose-nicotinamide[HYDROLASE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
Structural Basis for the Mechanism and Regulation of Sir2 Enzymes[TRANSCRIPTION]
Structure Of A Sir2 Enzyme Bound To An Acetylated P53 Peptide[Protein Binding, Transcription]
Sir2 homologue-ADP ribose complex[GENE REGULATION]
CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX[TRANSCRIPTION]
Sir2 homologue S24A mutant-ADP ribose complex[GENE REGULATION]
Sir2 homologue H80N mutant-ADP ribose complex[GENE REGULATION]
Sir2 homologue F159A mutant-ADP ribose complex[GENE REGULATION]
Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex[GENE REGULATION]
Structure of Sir2Tm bound to a propionylated peptide[HYDROLASE]
Sir2-S-alkylamidate complex crystal structure[HYDROLASE]
Crystal Structure Of Sir2tm In Complex With Acetyl P53 Peptide And Dadme-Nad+[Hydrolase, EC: 3.5.1.-]
The Structural basis of Sirtuin Substrate Affinity[HYDROLASE]
The Structural basis of sirtuin substrate specificity[HYDROLASE]
The Structural Basis of Sirtuin substrate affinity[HYDROLASE]
The Structural basis for Sirtuin Substrate affinity[HYDROLASE]
The Structural Basis for Sirtuin Substrate Affinity[HYDROLASE]
Sir2-deacetylated peptide (from enzymatic turnover in crystal)[HYDROLASE]
Sir2-p53 peptide-NAD+[HYDROLASE]
Sir2-P53 Peptide-Nicotinamide[Hydrolase, EC: 3.5.1.-]
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