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Potassium in PDB 1rxi: PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S

Enzymatic activity of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S

All present enzymatic activity of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S:
1.20.4.1;

Protein crystallography data

The structure of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S, PDB code: 1rxi was solved by J.Messens, I.Van Molle, P.Vanhaesebrouck, M.Limbourg, K.Vanbelle, K.Wahni, J.C.Martins, R.Loris, L.Wyns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.90 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 32.034, 34.064, 63.355, 90.00, 97.33, 90.00
R / Rfree (%) 20.9 / 23.1

Other elements in 1rxi:

The structure of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S (pdb code 1rxi). 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 PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S, PDB code: 1rxi:

Potassium binding site 1 out of 1 in 1rxi

Go back to Potassium Binding Sites List in 1rxi
Potassium binding site 1 out of 1 in the PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K151

b:15.8
occ:1.00
OD1 A:ASN13 2.8 11.8 1.0
O A:THR63 2.8 16.4 1.0
O A:SER36 2.9 12.5 1.0
OD2 A:ASP65 2.9 24.1 1.0
O A:HOH204 3.0 14.9 1.0
OG A:SER36 3.1 12.8 1.0
O A:HOH272 3.2 33.2 1.0
OE2 A:GLU21 3.6 18.0 1.0
C A:SER36 3.7 12.8 1.0
CG A:ASN13 3.8 12.8 1.0
CG A:ASP65 3.9 24.2 1.0
C A:THR63 3.9 19.3 1.0
ND2 A:ASN13 4.0 13.9 1.0
OG1 A:THR63 4.1 23.0 1.0
NE2 A:GLN18 4.1 13.6 1.0
N A:ASP65 4.2 17.3 1.0
CB A:ASP65 4.2 15.7 1.0
CB A:SER36 4.2 12.3 1.0
N A:SER36 4.2 10.7 1.0
CA A:SER36 4.3 9.8 1.0
O A:HOH250 4.5 29.8 1.0
N A:THR63 4.6 17.2 1.0
N A:ALA37 4.6 10.4 1.0
CD A:GLU21 4.6 20.0 1.0
OE1 A:GLN18 4.7 15.1 1.0
CA A:SER64 4.8 18.1 1.0
N A:SER64 4.8 18.2 1.0
CD A:GLN18 4.8 12.9 1.0
CA A:THR63 4.8 17.1 1.0
O A:HOH345 4.8 38.2 1.0
CA A:ASP65 4.8 19.5 1.0
C A:SER64 4.9 19.0 1.0
OE1 A:GLU21 4.9 22.8 1.0
CA A:ALA37 4.9 12.7 1.0
OD1 A:ASP65 5.0 25.6 1.0

Reference:

J.Messens, I.Van Molle, P.Vanhaesebrouck, K.Van Belle, K.Wahni, J.C.Martins, L.Wyns, R.Loris. The Structure of A Triple Mutant of PI258 Arsenate Reductase From Staphylococcus Aureus and Its 5-Thio-2-Nitrobenzoic Acid Adduct. Acta Crystallogr.,Sect.D V. 60 1180 2004.
ISSN: ISSN 0907-4449
PubMed: 15159594
DOI: 10.1107/S0907444904007334
Page generated: Mon Aug 12 05:18:22 2024

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