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Bromine in PDB 4c78: Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide

Enzymatic activity of Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide

All present enzymatic activity of Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide:
6.2.1.1;

Protein crystallography data

The structure of Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide, PDB code: 4c78 was solved by G.T.T.Nguyen, M.Gertz, M.Weyand, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.42 / 2.00
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.700, 52.600, 159.700, 90.00, 90.00, 90.00
R / Rfree (%) 19.375 / 24.056

Other elements in 4c78:

The structure of Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide (pdb code 4c78). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide, PDB code: 4c78:

Bromine binding site 1 out of 1 in 4c78

Go back to Bromine Binding Sites List in 4c78
Bromine binding site 1 out of 1 in the Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Complex of Human SIRT3 with Bromo-Resveratrol and ACS2 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1395

b:65.6
occ:1.00
BR A:BVB1395 0.0 65.6 1.0
CAO A:BVB1395 2.0 48.5 1.0
CAG A:BVB1395 2.9 33.9 1.0
CAF A:BVB1395 3.0 46.8 1.0
CAI A:BVB1395 4.2 31.6 1.0
CAH A:BVB1395 4.3 39.4 1.0
CAP A:BVB1395 4.8 38.1 1.0

Reference:

G.T.T.Nguyen, M.Gertz, C.Steegborn. Crystal Structures of SIRT3 Complexes with 4'-Bromo- Resveratrol Reveal Binding Sites and Inhibition Mechanism. Chem.Biol. V. 20 1375 2013.
ISSN: ISSN 1074-5521
PubMed: 24211137
DOI: 10.1016/J.CHEMBIOL.2013.09.019
Page generated: Sat Dec 12 02:18:39 2020

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