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Potassium in PDB 2fxi: Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site

Enzymatic activity of Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site

All present enzymatic activity of Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site:
3.1.3.48;

Protein crystallography data

The structure of Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site, PDB code: 2fxi was solved by R.Loris, L.Buts, J.Messens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.591, 33.579, 99.587, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.3

Potassium Binding Sites:

The binding sites of Potassium atom in the Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site (pdb code 2fxi). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site, PDB code: 2fxi:

Potassium binding site 1 out of 1 in 2fxi

Go back to Potassium Binding Sites List in 2fxi
Potassium binding site 1 out of 1 in the Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Arsenate Reductase (Arsc From PI258) C10S/C15A Double Mutant with Sulfate in Its Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K141

b:14.7
occ:1.00
 O A:THR63 2.8 13.1 1.0
O A:SER36 2.9 9.3 1.0
O A:HOH202 2.9 11.6 1.0
OD1 A:ASN13 2.9 9.4 1.0
OD2 A:ASP65 3.0 18.3 1.0
OG A:SER36 3.0 12.5 1.0
O A:HOH250 3.0 26.5 1.0
OE2 A:GLU21 3.5 13.9 1.0
C A:SER36 3.7 10.3 1.0
C A:THR63 3.9 14.7 1.0
CG A:ASN13 3.9 10.3 1.0
CG A:ASP65 3.9 18.0 1.0
OG1 A:THR63 4.1 16.0 1.0
ND2 A:ASN13 4.1 6.2 1.0
NE2 A:GLN18 4.1 7.9 1.0
CB A:SER36 4.1 12.1 1.0
N A:SER36 4.2 8.1 1.0
N A:ASP65 4.2 10.1 1.0
CA A:SER36 4.2 7.9 1.0
CB A:ASP65 4.2 13.9 1.0
CD A:GLU21 4.5 16.3 1.0
OE1 A:GLN18 4.5 11.8 1.0
N A:THR63 4.6 14.7 1.0
O A:HOH286 4.6 36.4 1.0
N A:ALA37 4.6 7.5 1.0
CD A:GLN18 4.7 11.9 1.0
O A:HOH216 4.7 18.3 1.0
CA A:THR63 4.7 15.5 1.0
OE1 A:GLU21 4.7 18.1 1.0
N A:SER64 4.8 12.9 1.0
CA A:SER64 4.8 11.5 1.0
CA A:ASP65 4.9 14.6 1.0
C A:SER64 4.9 12.8 1.0
OD1 A:ASP65 5.0 19.8 1.0
CA A:ALA37 5.0 8.1 1.0
CB A:THR63 5.0 15.2 1.0

Reference:

G.Roos, L.Buts, K.Van Belle, E.Brosens, P.Geerlings, R.Loris, L.Wyns, J.Messens. Interplay Between Ion Binding and Catalysis in the Thioredoxin-Coupled Arsenate Reductase Family. J.Mol.Biol. V. 360 826 2006.
ISSN: ISSN 0022-2836
PubMed: 16797027
DOI: 10.1016/J.JMB.2006.05.054
Page generated: Mon Aug 12 06:26:56 2024

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