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Zinc in PDB 3zs8: S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment

Enzymatic activity of S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment

All present enzymatic activity of S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment:
3.6.3.16;

Protein crystallography data

The structure of S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment, PDB code: 3zs8 was solved by M.Mariappan, A.Mateja, M.Dobosz, E.Bove, R.S.Hegde, R.J.Keenan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.215 / 3.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 110.276, 110.276, 315.956, 90.00, 90.00, 120.00
R / Rfree (%) 22.02 / 28.07

Zinc Binding Sites:

The binding sites of Zinc atom in the S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment (pdb code 3zs8). 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 S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment, PDB code: 3zs8:

Zinc binding site 1 out of 1 in 3zs8

Go back to Zinc Binding Sites List in 3zs8
Zinc binding site 1 out of 1 in the S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of S. Cerevisiae GET3 Complexed with A Cytosolic GET1 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1352

b:0.7
occ:1.00
SG A:CYS288 2.3 0.4 1.0
SG B:CYS285 2.3 0.7 1.0
SG A:CYS285 2.3 0.6 1.0
SG B:CYS288 2.3 0.3 1.0
CB B:CYS285 3.4 87.3 1.0
CB A:CYS285 3.4 81.2 1.0
CB A:CYS288 3.5 49.5 1.0
CB B:CYS288 3.5 65.6 1.0
N A:CYS288 3.7 86.6 1.0
N B:CYS288 3.8 85.8 1.0
CA A:CYS288 4.1 0.2 1.0
CA B:CYS288 4.1 0.7 1.0
CB A:ARG287 4.5 78.3 1.0
CB B:ARG287 4.5 61.5 1.0
C A:ARG287 4.7 0.9 1.0
CA B:CYS285 4.8 0.5 1.0
CA A:CYS285 4.8 0.2 1.0
C B:ARG287 4.8 0.9 1.0

Reference:

M.Mariappan, A.Mateja, M.Dobosz, E.Bove, R.S.Hegde, R.J.Keenan. The Mechanism of Membrane-Associated Steps in Tail-Anchored Protein Insertion. Nature V. 477 61 2011.
ISSN: ISSN 0028-0836
PubMed: 21866104
DOI: 10.1038/NATURE10362
Page generated: Wed Dec 16 04:59:53 2020

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