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Magnesium in PDB 3zs9: S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment

Enzymatic activity of S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment

All present enzymatic activity of S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment:
3.6.3.16;

Protein crystallography data

The structure of S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment, PDB code: 3zs9 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) 36.537 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.558, 77.317, 165.831, 90.00, 90.00, 90.00
R / Rfree (%) 18.22 / 23.8

Other elements in 3zs9:

The structure of S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Aluminium (Al) 2 atoms
Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment (pdb code 3zs9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment, PDB code: 3zs9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3zs9

Go back to Magnesium Binding Sites List in 3zs9
Magnesium binding site 1 out of 2 in the S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:18.1
occ:1.00
F2 A:ALF402 2.0 32.8 1.0
O3B A:ADP401 2.1 16.1 1.0
OG1 A:THR32 2.1 16.1 1.0
O A:HOH1402 2.1 24.1 1.0
O A:HOH1403 2.1 12.5 1.0
O A:HOH1401 2.1 10.1 1.0
F4 A:ALF402 2.9 42.0 1.0
CB A:THR32 3.1 15.3 1.0
AL A:ALF402 3.3 19.7 1.0
PB A:ADP401 3.4 14.4 1.0
O2B A:ADP401 3.4 12.5 1.0
N A:THR32 3.7 16.5 1.0
CA A:THR32 4.0 18.2 1.0
OD2 A:ASP57 4.0 16.6 1.0
OD2 A:ASP166 4.0 35.3 1.0
OD1 A:ASP166 4.0 29.6 1.0
OD1 A:ASN61 4.1 25.6 1.0
O3A A:ADP401 4.2 17.1 1.0
O2A A:ADP401 4.2 16.9 1.0
CG2 A:THR32 4.3 21.9 1.0
O A:HOH2020 4.3 21.9 1.0
O1B A:ADP401 4.3 22.2 1.0
O A:HOH2036 4.3 19.6 1.0
CB A:ASN61 4.4 12.6 1.0
F3 A:ALF402 4.4 20.1 1.0
CG A:ASP166 4.4 31.7 1.0
CB A:LYS31 4.6 13.5 1.0
O A:HOH2035 4.6 10.7 1.0
PA A:ADP401 4.7 18.0 1.0
O1A A:ADP401 4.7 16.9 1.0
CG A:ASN61 4.7 20.9 1.0
C A:LYS31 4.7 13.7 1.0
CE A:LYS31 4.8 18.9 1.0
F1 A:ALF402 4.9 30.3 1.0
O A:THR167 4.9 14.6 1.0
CG A:ASP57 5.0 16.8 1.0

Magnesium binding site 2 out of 2 in 3zs9

Go back to Magnesium Binding Sites List in 3zs9
Magnesium binding site 2 out of 2 in the S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:17.8
occ:1.00
F2 B:ALF402 2.0 26.2 1.0
O3B B:ADP401 2.1 12.7 1.0
O B:HOH1402 2.1 20.4 1.0
OG1 B:THR32 2.1 13.3 1.0
O B:HOH1401 2.1 18.1 1.0
O B:HOH1403 2.1 13.6 1.0
F4 B:ALF402 2.9 31.7 1.0
CB B:THR32 3.1 19.6 1.0
AL B:ALF402 3.3 24.7 1.0
PB B:ADP401 3.4 14.8 1.0
O2B B:ADP401 3.4 13.4 1.0
N B:THR32 3.8 16.3 1.0
CA B:THR32 4.0 23.1 1.0
OD2 B:ASP166 4.0 24.1 1.0
OD2 B:ASP57 4.0 19.1 1.0
OD1 B:ASP166 4.2 27.6 1.0
ND2 B:ASN61 4.2 24.9 1.0
O2A B:ADP401 4.2 19.7 1.0
O3A B:ADP401 4.2 18.1 1.0
O B:HOH2018 4.2 22.4 1.0
CG2 B:THR32 4.3 16.1 1.0
O1B B:ADP401 4.3 15.8 1.0
O A:HOH2085 4.4 23.0 1.0
F3 B:ALF402 4.4 27.2 1.0
O B:HOH2029 4.5 18.6 1.0
CB B:ASN61 4.5 16.2 1.0
CG B:ASP166 4.5 28.3 1.0
CB B:LYS31 4.7 16.6 1.0
PA B:ADP401 4.7 15.0 1.0
O1A B:ADP401 4.8 12.8 1.0
C B:LYS31 4.8 21.6 1.0
F1 B:ALF402 4.9 28.3 1.0
CG B:ASN61 4.9 26.8 1.0
CE B:LYS31 4.9 18.9 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: Mon Dec 14 09:04:25 2020

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