Arsenic in PDB 1nw2: The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius

All present enzymatic activity of The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius:
1.8.1.9;

The structure of The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius, PDB code: 1nw2 was solved by S.Bartolucci, G.De Simone, S.Galdiero, R.Improta, V.Menchise, C.Pedone, E.Pedone, M.Saviano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	79.610, 60.210, 82.950, 90.00, 93.30, 90.00
R / Rfree (%)	21.2 / 25.5

The structure of The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius also contains other interesting chemical elements:

Zinc

(Zn)

9 atoms

The binding sites of Arsenic atom in the The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius (pdb code 1nw2). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius, PDB code: 1nw2:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius within 5.0Å range: probe atom residue distance (Å) B Occ D:As5001 b:22.0 occ:1.00 AS D:CAC5001 0.0 22.0 1.0 O2 D:CAC5001 1.8 24.2 1.0 O1 D:CAC5001 1.8 23.3 1.0 C1 D:CAC5001 1.9 23.0 1.0 C2 D:CAC5001 1.9 23.4 1.0 ZN D:ZN6004 3.3 19.1 1.0 ZN D:ZN6009 3.4 19.7 1.0 O1 D:CAC5002 3.6 24.8 1.0 OE2 D:GLU97 3.6 11.0 1.0 O D:HOH6027 3.9 20.5 1.0 C1 D:CAC5002 4.2 24.4 1.0 AS D:CAC5002 4.3 23.6 1.0 O2 D:CAC5002 4.4 23.0 1.0 CB D:ALA101 4.5 16.2 1.0 CD D:GLU97 4.9 12.4 1.0 O D:HOH6039 5.0 33.5 1.0 NE2 D:HIS46 5.0 15.9 1.0

Arsenic binding site 2 out of 2 in the The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of The Crystal Structure of the Mutant R82E of Thioredoxin From Alicyclobacillus Acidocaldarius within 5.0Å range: probe atom residue distance (Å) B Occ D:As5002 b:23.6 occ:1.00 AS D:CAC5002 0.0 23.6 1.0 O2 D:CAC5002 1.8 23.0 1.0 O1 D:CAC5002 1.8 24.8 1.0 C1 D:CAC5002 1.9 24.4 1.0 C2 D:CAC5002 1.9 24.3 1.0 ZN D:ZN6009 3.2 19.7 1.0 ZN D:ZN6004 3.2 19.1 1.0 O2 D:CAC5001 3.3 24.2 1.0 O D:HOH6092 3.7 27.0 1.0 O D:HOH6040 3.9 26.3 1.0 AS D:CAC5001 4.3 22.0 1.0 O D:HOH6020 4.3 15.3 1.0 NE2 D:HIS46 4.3 15.9 1.0 O1 D:CAC5001 4.3 23.3 1.0 C1 D:CAC5001 4.5 23.0 1.0 OE2 D:GLU97 4.6 11.0 1.0 O F:HOH7015 4.9 23.6 1.0 O D:ALA45 4.9 16.4 1.0 OE1 D:GLU97 5.0 11.9 1.0 CE1 D:HIS46 5.0 15.3 1.0

S.Bartolucci, G.De Simone, S.Galdiero, R.Improta, V.Menchise, C.Pedone, E.Pedone, M.Saviano. An Integrated Structural and Computational Study of the Thermostability of Two Thioredoxin Mutants From Alicyclobacillus Acidocaldarius J.Bacteriol. V. 185 4285 2003.
ISSN: ISSN 0021-9193
PubMed: 12837806
DOI: 10.1128/JB.185.14.4285-4289.2003