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Zinc in PDB 4fvt: Human SIRT3 Bound to Ac-Acs Peptide and Carba-Nad

Protein crystallography data

The structure of Human SIRT3 Bound to Ac-Acs Peptide and Carba-Nad, PDB code: 4fvt was solved by H.Dai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.72 / 2.47
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 77.430, 131.050, 77.320, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 24.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Human SIRT3 Bound to Ac-Acs Peptide and Carba-Nad (pdb code 4fvt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human SIRT3 Bound to Ac-Acs Peptide and Carba-Nad, PDB code: 4fvt:

Zinc binding site 1 out of 1 in 4fvt

Go back to Zinc Binding Sites List in 4fvt
Zinc binding site 1 out of 1 in the Human SIRT3 Bound to Ac-Acs Peptide and Carba-Nad


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human SIRT3 Bound to Ac-Acs Peptide and Carba-Nad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:48.5
occ:1.00
SG A:CYS259 2.2 49.0 1.0
SG A:CYS280 2.3 45.2 1.0
SG A:CYS283 2.3 50.8 1.0
SG A:CYS256 2.4 51.0 1.0
CB A:CYS280 3.0 48.6 1.0
CB A:CYS256 3.2 46.7 1.0
CB A:CYS259 3.2 47.7 1.0
CB A:CYS283 3.5 52.9 1.0
N A:CYS259 3.7 50.7 1.0
N A:CYS283 3.9 54.3 1.0
CA A:CYS259 4.0 49.6 1.0
CA A:CYS283 4.2 55.2 1.0
CA A:CYS280 4.5 51.0 1.0
N A:GLY285 4.5 47.3 1.0
CA A:CYS256 4.7 46.1 1.0
CB A:VAL258 4.7 55.5 1.0
C A:CYS283 4.7 53.8 1.0
C A:VAL258 4.8 52.0 1.0
CA A:GLY285 4.8 45.1 1.0
C A:CYS259 4.8 50.8 1.0
NH2 A:ARG261 4.9 61.8 1.0
N A:THR284 4.9 50.3 1.0
CD A:ARG261 4.9 66.2 1.0
CB A:ARG261 5.0 53.8 1.0

Reference:

B.G.Szczepankiewicz, H.Dai, K.J.Koppetsch, D.Qian, F.Jiang, C.Mao, R.B.Perni. Synthesis of Carba-Nad and the Structures of Its Ternary Complexes with SIRT3 and SIRT5. J.Org.Chem. V. 77 7319 2012.
ISSN: ISSN 0022-3263
PubMed: 22849721
DOI: 10.1021/JO301067E
Page generated: Wed Dec 16 05:18:18 2020

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