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Aluminium 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
Magnesium (Mg) 2 atoms
Zinc (Zn) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium 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 Aluminium atom.
In total 2 binding sites of Aluminium where determined in the S. Cerevisiae GET3-Adp-ALF4- Complex with A Cytosolic GET2 Fragment, PDB code: 3zs9:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 3zs9

Go back to Aluminium Binding Sites List in 3zs9
Aluminium 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 Aluminium with other atoms in the Al 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:Al402

b:19.7
occ:1.00
AL A:ALF402 0.0 19.7 1.0
F3 A:ALF402 1.8 20.1 1.0
F4 A:ALF402 1.8 42.0 1.0
F2 A:ALF402 1.8 32.8 1.0
F1 A:ALF402 1.8 30.3 1.0
O2B A:ADP401 1.9 12.5 1.0
O A:HOH2035 2.2 10.7 1.0
PB A:ADP401 3.2 14.4 1.0
MG A:MG403 3.3 18.1 1.0
O3B A:ADP401 3.5 16.1 1.0
NZ B:LYS26 3.7 12.3 1.0
OD2 A:ASP57 3.7 16.6 1.0
O A:HOH1403 3.7 12.5 1.0
O A:HOH2036 3.7 19.6 1.0
O A:HOH1402 4.0 24.1 1.0
O1B A:ADP401 4.0 22.2 1.0
N A:GLY28 4.1 14.6 1.0
O B:HOH2016 4.1 19.4 1.0
NZ A:LYS31 4.2 17.1 1.0
O3A A:ADP401 4.3 17.1 1.0
O A:HOH1401 4.3 10.1 1.0
N B:GLY27 4.4 17.8 1.0
CE B:LYS26 4.4 12.1 1.0
CA B:GLY27 4.5 11.8 1.0
CG A:PRO169 4.5 14.7 1.0
CG B:LYS26 4.5 12.4 1.0
CE A:LYS31 4.5 18.9 1.0
OD1 A:ASN61 4.7 25.6 1.0
CA A:GLY28 4.7 13.4 1.0
CD A:PRO169 4.7 16.2 1.0
O2A A:ADP401 4.8 16.9 1.0
CA A:GLY27 4.8 15.6 1.0
CG A:ASP57 4.9 16.8 1.0
C A:GLY27 5.0 16.9 1.0

Aluminium binding site 2 out of 2 in 3zs9

Go back to Aluminium Binding Sites List in 3zs9
Aluminium 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 Aluminium with other atoms in the Al 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:Al402

b:24.7
occ:1.00
AL B:ALF402 0.0 24.7 1.0
F1 B:ALF402 1.8 28.3 1.0
F4 B:ALF402 1.8 31.7 1.0
F2 B:ALF402 1.8 26.2 1.0
F3 B:ALF402 1.8 27.2 1.0
O2B B:ADP401 1.9 13.4 1.0
O B:HOH2029 2.2 18.6 1.0
PB B:ADP401 3.2 14.8 1.0
MG B:MG403 3.3 17.8 1.0
O3B B:ADP401 3.5 12.7 1.0
NZ A:LYS26 3.5 16.0 1.0
O B:HOH1403 3.7 13.6 1.0
O A:HOH2085 3.7 23.0 1.0
OD2 B:ASP57 3.9 19.1 1.0
O1B B:ADP401 4.0 15.8 1.0
N B:GLY28 4.0 19.3 1.0
NZ B:LYS31 4.1 16.8 1.0
O A:HOH2017 4.1 15.0 1.0
O B:HOH1402 4.1 20.4 1.0
O3A B:ADP401 4.2 18.1 1.0
O B:HOH1401 4.3 18.1 1.0
CE A:LYS26 4.3 16.9 1.0
N A:GLY27 4.4 15.9 1.0
CG A:LYS26 4.5 11.4 1.0
CG B:PRO169 4.5 19.1 1.0
CA A:GLY27 4.6 15.6 1.0
CA B:GLY28 4.6 12.0 1.0
CE B:LYS31 4.7 18.9 1.0
O2A B:ADP401 4.7 19.7 1.0
ND2 B:ASN61 4.9 24.9 1.0
CD B:PRO169 4.9 17.4 1.0
CA B:GLY27 4.9 11.8 1.0
C B:GLY27 5.0 14.4 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 Jul 10 09:43:00 2024

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