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Arsenic in PDB 3fpl: Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh

Enzymatic activity of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh

All present enzymatic activity of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh:
1.1.1.2;

Protein crystallography data

The structure of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh, PDB code: 3fpl was solved by F.Felix, E.Goihberg, L.Shimon, Y.Burstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 1.90
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 129.477, 129.477, 129.477, 90.00, 90.00, 90.00
R / Rfree (%) 12.2 / 17.2

Other elements in 3fpl:

The structure of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Zinc (Zn) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh (pdb code 3fpl). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh, PDB code: 3fpl:

Arsenic binding site 1 out of 1 in 3fpl

Go back to Arsenic Binding Sites List in 3fpl
Arsenic binding site 1 out of 1 in the Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Chimera of Alcohol Dehydrogenase By Exchange of the Cofactor Binding Domain Res 153-295 of C. Beijerinckii Adh By T. Brockii Adh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As356

b:24.0
occ:1.00
 AS A:CAC356 0.0 24.0 1.0
O1 A:CAC356 1.7 22.1 1.0
O2 A:CAC356 1.8 22.9 1.0
C1 A:CAC356 1.9 24.3 1.0
C2 A:CAC356 2.0 22.7 1.0
ZN A:ZN352 3.3 23.9 1.0
OD1 A:ASP150 3.6 21.1 1.0
O A:HOH393 3.7 17.4 1.0
OG A:SER39 3.7 20.2 1.0
O A:HOH649 3.8 30.6 1.0
OD2 A:ASP150 3.8 20.5 1.0
CG A:ASP150 4.1 22.1 1.0
NE2 A:HIS59 4.1 19.8 1.0
CB A:SER39 4.5 21.3 1.0
O A:HOH709 4.7 38.1 1.0
CE2 A:TRP110 4.7 18.8 1.0
CZ2 A:TRP110 4.7 26.7 1.0
CD2 A:HIS59 4.7 21.3 1.0
OG1 A:THR154 4.7 15.7 1.0
CD1 A:LEU294 4.8 16.1 1.0
CE1 A:HIS59 4.9 20.1 1.0
CD2 A:TRP110 4.9 20.5 1.0
CH2 A:TRP110 4.9 23.1 1.0
SG A:CYS37 5.0 19.7 1.0

Reference:

E.Goihberg, M.Peretz, S.Tel-Or, O.Dym, L.Shimon, F.Frolow, Y.Burstein. Biochemical and Structural Properties of Chimeras Constructed By Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases From Thermophilic and Mesophilic Microorganisms Biochemistry V. 49 1943 2010.
ISSN: ISSN 0006-2960
PubMed: 20102159
DOI: 10.1021/BI901730X
Page generated: Wed Jul 10 11:41:01 2024

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