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Zinc in PDB 8ccw: Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide

Enzymatic activity of Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide

All present enzymatic activity of Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide:
2.3.1.286;

Protein crystallography data

The structure of Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide, PDB code: 8ccw was solved by R.S.Adolph, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.36 / 1.65
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 78.721, 127.76, 77.576, 90, 90, 90
R / Rfree (%) 18.1 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide (pdb code 8ccw). 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 Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide, PDB code: 8ccw:

Zinc binding site 1 out of 1 in 8ccw

Go back to Zinc Binding Sites List in 8ccw
Zinc binding site 1 out of 1 in the Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human SIRT3 in Complex with An Acetylated HIV1 Tat-46-54 Substrate Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:26.9
occ:1.00
 SG A:CYS280 2.3 26.2 1.0
SG A:CYS283 2.3 28.4 1.0
SG A:CYS259 2.3 30.1 1.0
SG A:CYS256 2.4 25.4 1.0
CB A:CYS280 3.0 24.0 1.0
CB A:CYS256 3.2 27.0 1.0
CB A:CYS259 3.2 25.4 1.0
CB A:CYS283 3.5 27.5 1.0
N A:CYS259 3.7 25.6 1.0
N A:CYS283 3.9 26.7 1.0
CA A:CYS259 4.0 29.3 1.0
CA A:CYS283 4.2 25.0 1.0
CA A:CYS280 4.5 24.5 1.0
N A:GLY285 4.5 25.0 1.0
CA A:CYS256 4.6 25.4 1.0
C A:CYS283 4.7 25.3 1.0
C A:CYS259 4.8 35.2 1.0
N A:THR284 4.8 24.0 1.0
CB A:VAL258 4.8 28.8 1.0
C A:VAL258 4.9 31.6 1.0
CB A:ARG261 4.9 35.5 1.0
N A:GLN260 4.9 29.3 1.0
CA A:GLY285 4.9 25.4 1.0
C A:VAL282 5.0 31.9 1.0
CB A:VAL282 5.0 30.4 1.0

Reference:

R.S.Adolph, E.Beck, K.Schweimer, A.Di Fonzo, M.Weyand, P.Rosch, B.M.Wohrl, C.Steegborn. Molecular Mechanism of Sirtuin 1 Inhibition By Human Immunodeficiency Virus 1 Tat Protein. Life V. 13 2023.
ISSN: ESSN 2075-1729
PubMed: 37109478
DOI: 10.3390/LIFE13040949
Page generated: Fri Aug 22 08:53:03 2025

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