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Potassium in PDB 1lju: X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite

Enzymatic activity of X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite

All present enzymatic activity of X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite:
1.97.1.5;

Protein crystallography data

The structure of X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite, PDB code: 1lju was solved by I.Zegers, J.C.Martins, R.Willem, L.Wyns, J.Messens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.94 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.970, 37.830, 106.370, 90.00, 90.00, 90.00
R / Rfree (%) 24.1 / 26.7

Other elements in 1lju:

The structure of X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite also contains other interesting chemical elements:

Arsenic (As) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite (pdb code 1lju). 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 X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite, PDB code: 1lju:

Potassium binding site 1 out of 1 in 1lju

Go back to Potassium Binding Sites List in 1lju
Potassium binding site 1 out of 1 in the X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of X-Ray Structure of C15A Arsenate Reductase From PI258 Complexed with Arsenite within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K134

b:14.6
occ:1.00
 O A:THR63 2.7 13.5 1.0
O A:SER36 2.8 14.0 1.0
OD2 A:ASP65 2.8 19.0 1.0
O A:HOH141 2.8 15.5 1.0
OD1 A:ASN13 2.9 12.4 1.0
OG A:SER36 2.9 13.3 1.0
O A:HOH158 3.1 23.6 1.0
OE2 A:GLU21 3.1 20.8 1.0
CG A:ASP65 3.6 17.2 1.0
C A:SER36 3.7 12.6 1.0
CG A:ASN13 3.8 12.1 1.0
C A:THR63 3.9 13.6 1.0
ND2 A:ASN13 4.0 12.1 1.0
NE2 A:GLN18 4.0 12.4 1.0
CB A:SER36 4.0 13.9 1.0
O A:HOH253 4.1 46.7 1.0
O A:HOH146 4.1 19.2 1.0
N A:SER36 4.1 12.2 1.0
CA A:SER36 4.1 12.5 1.0
CB A:ASP65 4.2 15.8 1.0
N A:ASP65 4.2 12.5 1.0
CD A:GLU21 4.2 17.5 1.0
OE1 A:GLN18 4.4 13.9 1.0
OG1 A:THR63 4.4 17.7 1.0
OD1 A:ASP65 4.5 20.8 1.0
OE1 A:GLU21 4.5 19.3 1.0
CD A:GLN18 4.6 10.0 1.0
N A:THR63 4.6 18.0 1.0
CA A:SER64 4.7 13.5 1.0
N A:SER64 4.7 13.6 1.0
N A:ALA37 4.7 11.7 1.0
CA A:THR63 4.8 15.8 1.0
CA A:ASP65 4.8 13.9 1.0
C A:SER64 4.9 14.2 1.0

Reference:

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
Page generated: Mon Aug 12 04:50:53 2024

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