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Zinc 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:

Arsenic (As) 1 atom
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc 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:

Zinc binding site 1 out of 1 in 3fpl

Go back to Zinc Binding Sites List in 3fpl
Zinc 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 Zinc with other atoms in the Zn 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:Zn352

b:23.9
occ:1.00
 OD2 A:ASP150 2.0 20.5 1.0
O1 A:CAC356 2.0 22.1 1.0
NE2 A:HIS59 2.1 19.8 1.0
SG A:CYS37 2.2 19.7 1.0
CD2 A:HIS59 3.0 21.3 1.0
CE1 A:HIS59 3.1 20.1 1.0
CG A:ASP150 3.1 22.1 1.0
CB A:CYS37 3.2 21.1 1.0
AS A:CAC356 3.3 24.0 1.0
OD1 A:ASP150 3.6 21.1 1.0
OG A:SER39 3.7 20.2 1.0
O2 A:CAC356 3.9 22.9 1.0
CB A:SER39 3.9 21.3 1.0
O A:HOH649 3.9 30.6 1.0
C1 A:CAC356 4.0 24.3 1.0
OE2 A:GLU60 4.1 22.8 1.0
ND1 A:HIS59 4.2 19.0 1.0
CG A:HIS59 4.2 16.4 1.0
CE A:MET151 4.3 10.4 1.0
CB A:ASP150 4.3 17.3 1.0
CD A:GLU60 4.5 21.6 1.0
CA A:CYS37 4.6 19.0 1.0
N A:SER39 4.9 20.4 1.0
O A:HOH632 4.9 26.1 1.0
C2 A:CAC356 4.9 22.7 1.0
OE1 A:GLU60 4.9 16.4 1.0
CG A:GLU60 5.0 22.2 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: Thu Oct 24 13:22:20 2024

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