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Sodium in PDB 2fwe: Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form)

Enzymatic activity of Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form)

All present enzymatic activity of Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form):
1.8.1.8;

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form), PDB code: 2fwe was solved by C.U.Stirnimann, A.Rozhkova, U.Grauschopf, R.A.Boeckmann, R.Glockshuber, G.Capitani, M.G.Gruetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 30.265, 45.961, 73.768, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 23.5

Other elements in 2fwe:

The structure of Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form) also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Iodine (I) 11 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form) (pdb code 2fwe). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form), PDB code: 2fwe:

Sodium binding site 1 out of 1 in 2fwe

Go back to Sodium Binding Sites List in 2fwe
Sodium binding site 1 out of 1 in the Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the C-Terminal Domain of the Electron Transfer Catalyst Dsbd (Oxidized Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1101

b:21.1
occ:0.70
I A:IOD1002 1.9 19.4 0.1
O A:HOH126 3.0 21.5 1.0
O A:HOH77 3.1 24.3 1.0
N A:GLN545 3.1 24.9 1.0
I A:IOD1002 3.3 13.6 0.7
CB A:HIS523 3.6 11.6 1.0
CA A:ARG544 3.7 19.9 1.0
C A:ARG544 3.8 22.5 1.0
CG A:HIS523 3.8 13.7 1.0
CB A:GLN545 3.9 26.6 1.0
CD2 A:HIS523 4.0 13.2 1.0
CA A:GLN545 4.1 25.5 1.0
CB A:ALA526 4.1 13.2 1.0
CB A:ARG544 4.1 10.3 1.0
CG A:ARG544 4.4 12.9 1.0
O A:HOH19 4.4 16.4 0.1
ND1 A:HIS523 4.7 15.3 1.0
NE2 A:GLN525 4.7 24.5 1.0
O A:ASP543 4.8 25.1 1.0
N A:ARG544 4.9 24.5 1.0
NE2 A:HIS523 4.9 14.5 1.0

Reference:

C.U.Stirnimann, A.Rozhkova, U.Grauschopf, R.A.Boeckmann, R.Glockshuber, G.Capitani, M.G.Gruetter. High-Resolution Structures of Escherichia Coli Cdsbd in Different Redox States: A Combined Crystallographic, Biochemical and Computational Study J.Mol.Biol. V. 358 829 2006.
ISSN: ISSN 0022-2836
PubMed: 16545842
DOI: 10.1016/J.JMB.2006.02.030
Page generated: Tue Dec 15 05:49:18 2020

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