Potassium in PDB 1ljl: Wild Type PI258 S. Aureus Arsenate Reductase

All present enzymatic activity of Wild Type PI258 S. Aureus Arsenate Reductase:
1.97.1.5;

The structure of Wild Type PI258 S. Aureus Arsenate Reductase, PDB code: 1ljl was solved by J.Messens, J.C.Martins, K.Van Belle, E.Brosens, A.Desmyter, M.De Gieter, J.M.Wieruszeski, R.Willem, L.Wyns, I.Zegers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.96 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.450, 32.770, 100.920, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 25.9

The binding sites of Potassium atom in the Wild Type PI258 S. Aureus Arsenate Reductase (pdb code 1ljl). 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 Wild Type PI258 S. Aureus Arsenate Reductase, PDB code: 1ljl:

Potassium binding site 1 out of 1 in the Wild Type PI258 S. Aureus Arsenate Reductase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Wild Type PI258 S. Aureus Arsenate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:K133 b:30.2 occ:1.00 O A:HOH143 2.6 30.9 1.0 O A:SER36 2.7 22.1 1.0 O A:THR63 2.7 23.6 1.0 OD2 A:ASP65 2.8 26.8 1.0 OD1 A:ASN13 2.9 22.9 1.0 O A:HOH136 2.9 25.2 1.0 OG A:SER36 3.1 22.1 1.0 C A:SER36 3.5 21.2 1.0 CG A:ASN13 3.8 22.4 1.0 C A:THR63 3.8 24.8 1.0 CG A:ASP65 3.9 25.1 1.0 O A:HOH148 3.9 37.6 1.0 OE2 A:GLU21 4.0 28.5 1.0 ND2 A:ASN13 4.0 21.7 1.0 NE2 A:GLN18 4.1 22.8 1.0 CA A:SER36 4.1 21.0 1.0 CB A:SER36 4.1 19.6 1.0 N A:SER36 4.2 20.0 1.0 N A:ASP65 4.2 24.9 1.0 OG1 A:THR63 4.3 24.4 1.0 CB A:ASP65 4.3 25.4 1.0 N A:ALA37 4.5 21.8 1.0 N A:THR63 4.6 26.4 1.0 O A:HOH184 4.6 44.6 1.0 CA A:THR63 4.7 25.2 1.0 OE1 A:GLN18 4.7 23.5 1.0 N A:SER64 4.7 24.8 1.0 CA A:SER64 4.8 25.9 1.0 CD A:GLN18 4.8 22.5 1.0 CD A:GLU21 4.8 25.4 1.0 CA A:ASP65 4.9 24.7 1.0 CA A:ALA37 4.9 23.3 1.0 C A:SER64 4.9 25.5 1.0 OD1 A:ASP65 5.0 26.4 1.0 OE1 A:GLU21 5.0 26.8 1.0

J.Messens, J.C.Martins, K.Van Belle, E.Brosens, A.Desmyter, M.De Gieter, J.M.Wieruszeski, R.Willem, L.Wyns, I.Zegers. All Intermediates of the Arsenate Reductase Mechanism, Including An Intramolecular Dynamic Disulfide Cascade. Proc.Natl.Acad.Sci.Usa V. 99 8506 2002.
ISSN: ISSN 0027-8424
PubMed: 12072565
DOI: 10.1073/PNAS.132142799