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Zinc in PDB 3glr: Crystal Structure of Human SIRT3 with Acetyl-Lysine ACECS2 Peptide

Enzymatic activity of Crystal Structure of Human SIRT3 with Acetyl-Lysine ACECS2 Peptide

All present enzymatic activity of Crystal Structure of Human SIRT3 with Acetyl-Lysine ACECS2 Peptide:
6.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Human SIRT3 with Acetyl-Lysine ACECS2 Peptide, PDB code: 3glr 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 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 78.190, 129.063, 77.899, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 22.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human SIRT3 with Acetyl-Lysine ACECS2 Peptide (pdb code 3glr). 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 Acetyl-Lysine ACECS2 Peptide, PDB code: 3glr:

Zinc binding site 1 out of 1 in 3glr

Go back to Zinc Binding Sites List in 3glr
Zinc binding site 1 out of 1 in the Crystal Structure of Human SIRT3 with Acetyl-Lysine ACECS2 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 with Acetyl-Lysine ACECS2 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:18.8
occ:1.00
SG A:CYS280 2.3 18.1 1.0
SG A:CYS283 2.3 20.1 1.0
SG A:CYS259 2.3 19.1 1.0
SG A:CYS256 2.4 18.2 1.0
CB A:CYS280 3.1 16.3 1.0
CB A:CYS256 3.1 15.5 1.0
CB A:CYS259 3.3 18.9 1.0
CB A:CYS283 3.5 18.1 1.0
N A:CYS259 3.7 17.7 1.0
N A:CYS283 3.9 18.9 1.0
CA A:CYS259 4.0 19.5 1.0
CA A:CYS283 4.2 18.6 1.0
N A:GLY285 4.5 15.6 1.0
CA A:CYS280 4.5 16.5 1.0
CA A:CYS256 4.6 15.5 1.0
C A:CYS283 4.7 17.8 1.0
C A:CYS259 4.8 20.0 1.0
N A:THR284 4.8 16.8 1.0
CB A:VAL258 4.9 17.7 1.0
C A:VAL258 4.9 18.9 1.0
C A:VAL282 4.9 21.5 1.0
N A:GLN260 4.9 19.4 1.0
CB A:VAL282 4.9 20.0 1.0
CB A:ARG261 5.0 22.3 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 13:46:23 2024

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