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Zinc in PDB 3glt: Crystal Structure of Human SIRT3 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine

Enzymatic activity of Crystal Structure of Human SIRT3 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine

All present enzymatic activity of Crystal Structure of Human SIRT3 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine:
6.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Human SIRT3 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine, PDB code: 3glt was solved by L.Jin, W.Wei, Y.Jiang, H.Peng, J.Cai, C.Mao, H.Dai, J.E.Bemis, M.R.Jirousek, J.C.Milne, C.H.Westphal, R.B.Perni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.00 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 80.718, 127.281, 76.831, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 22.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human SIRT3 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine (pdb code 3glt). 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 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine, PDB code: 3glt:

Zinc binding site 1 out of 1 in 3glt

Go back to Zinc Binding Sites List in 3glt
Zinc binding site 1 out of 1 in the Crystal Structure of Human SIRT3 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine


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 with Adpr Bound to the ACECS2 Peptide Containing A Thioacetyl Lysine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:13.0
occ:1.00
 SG A:CYS283 2.2 12.5 1.0
SG A:CYS280 2.3 12.3 1.0
SG A:CYS259 2.3 15.4 1.0
SG A:CYS256 2.4 11.2 1.0
CB A:CYS280 3.1 11.7 1.0
CB A:CYS256 3.1 10.5 1.0
CB A:CYS259 3.3 15.2 1.0
CB A:CYS283 3.5 12.9 1.0
N A:CYS259 3.7 15.4 1.0
N A:CYS283 3.9 14.4 1.0
CA A:CYS259 4.1 15.7 1.0
CA A:CYS283 4.2 13.4 1.0
CD A:ARG261 4.3 29.0 0.5
N A:GLY285 4.5 11.8 1.0
CA A:CYS280 4.5 11.8 1.0
CB A:VAL282 4.5 18.9 1.0
CA A:CYS256 4.6 9.2 1.0
C A:CYS283 4.7 13.7 1.0
C A:VAL282 4.8 18.2 1.0
C A:CYS259 4.8 17.6 1.0
CB A:VAL258 4.8 12.6 1.0
CG1 A:VAL282 4.8 24.4 1.0
CA A:GLY285 4.9 12.0 1.0
N A:THR284 4.9 12.6 1.0
C A:VAL258 4.9 16.1 1.0
N A:GLN260 5.0 17.1 1.0

Reference:

L.Jin, W.Wei, Y.Jiang, H.Peng, J.Cai, C.Mao, H.Dai, W.Choy, J.E.Bemis, M.R.Jirousek, J.C.Milne, C.H.Westphal, R.B.Perni. Crystal Structures of Human SIRT3 Displaying Substrate-Induced Conformational Changes. J.Biol.Chem. V. 284 24394 2009.
ISSN: ISSN 0021-9258
PubMed: 19535340
DOI: 10.1074/JBC.M109.014928
Page generated: Thu Oct 24 13:49:02 2024

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