PDBsum entry 4fvt

Hydrolase

PDB id: 4fvt

Contents

Protein chain

274 a.a.

Ligands

SER-GLY-ALY-VAL-NLE

CNA

SO4 ×3

GOL

Metals

_ZN

Waters ×55

PDB id:

4fvt

Name:

Hydrolase

Title:

Human sirt3 bound to ac-acs peptide and carba-NAD

Structure:

NAD-dependent protein deacetylase sirtuin-3, mitochondrial. Chain: a. Fragment: unp residues 122-395. Synonym: hsirt3, regulatory protein sir2 homolog 3, sir2-like protein 3. Engineered: yes. Acetylated acs2 peptide. Chain: b. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic ac-acs2 peptide

Resolution:

2.47Å R-factor: 0.204 R-free: 0.249

Authors:

H.Dai

Key ref:

B.G.Szczepankiewicz et al. (2012). Synthesis of carba-NAD and the structures of its ternary complexes with SIRT3 and SIRT5. J Org Chem, 77, 7319-7329. PubMed id: 22849721

Date:

29-Jun-12 Release date: 15-Aug-12

Protein chain

Q9NTG7  (SIR3_HUMAN) -  NAD-dependent protein deacetylase sirtuin-3, mitochondrial from Homo sapiens

Seq: 399 a.a.

Struc: 274 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.286 - protein acetyllysine N-acetyltransferase.
• Reaction: N₆-acetyl-L-lysyl-[protein] + NAD⁺ + H2O = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]

N(6)-acetyl-L-lysyl-[protein] + NAD(+) + H2O (Bound ligand (Het Group name = CNA) matches with 95.56% similarity) = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein] (Bound ligand (Het Group name = ALY) matches with 61.54% similarity)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

J Org Chem 77:7319-7329 (2012)

PubMed id: 22849721

Synthesis of carba-NAD and the structures of its ternary complexes with SIRT3 and SIRT5.

B.G.Szczepankiewicz, H.Dai, K.J.Koppetsch, D.Qian, F.Jiang, C.Mao, R.B.Perni.

ABSTRACT

No abstract given.