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Zinc in PDB 2oxi: Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution

Enzymatic activity of Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution

All present enzymatic activity of Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution:
1.1.1.1;

Protein crystallography data

The structure of Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution, PDB code: 2oxi was solved by S.Al-Karadaghi, E.S.Cedergren-Zeppezauer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.400, 180.600, 50.800, 90.00, 108.00, 90.00
R / Rfree (%) 16 / n/a

Other elements in 2oxi:

The structure of Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution (pdb code 2oxi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution, PDB code: 2oxi:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2oxi

Go back to Zinc Binding Sites List in 2oxi
Zinc binding site 1 out of 2 in the Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:24.4
occ:1.00
SG A:CYS103 2.2 22.4 1.0
SG A:CYS111 2.3 24.7 1.0
SG A:CYS100 2.3 25.6 1.0
SG A:CYS97 2.5 35.2 1.0
CB A:CYS103 3.3 24.3 1.0
CB A:CYS111 3.4 21.2 1.0
CB A:CYS100 3.4 25.3 1.0
N A:CYS97 3.4 28.6 1.0
CB A:CYS97 3.5 31.9 1.0
N A:CYS100 3.7 31.7 1.0
CA A:CYS111 3.8 20.6 1.0
CA A:CYS97 3.9 31.4 1.0
N A:GLY98 3.9 31.6 1.0
N A:LEU112 4.0 23.7 1.0
N A:CYS103 4.1 24.8 1.0
C A:CYS97 4.1 33.8 1.0
CA A:CYS100 4.2 28.7 1.0
CA A:CYS103 4.3 25.2 1.0
C A:CYS111 4.3 22.9 1.0
C A:GLN96 4.4 25.7 1.0
N A:LYS99 4.5 30.8 1.0
C A:CYS100 4.8 27.9 1.0
O A:CYS100 4.8 28.0 1.0
N A:LYS113 4.9 26.5 1.0
C A:LYS99 4.9 34.4 1.0
CA A:GLY98 4.9 30.7 1.0
CA A:GLN96 4.9 25.4 1.0
CG A:LYS113 5.0 35.0 1.0

Zinc binding site 2 out of 2 in 2oxi

Go back to Zinc Binding Sites List in 2oxi
Zinc binding site 2 out of 2 in the Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Refined Crystal Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:19.9
occ:1.00
SG B:CYS103 2.2 18.1 1.0
SG B:CYS100 2.3 21.1 1.0
SG B:CYS111 2.3 17.7 1.0
SG B:CYS97 2.4 23.3 1.0
CB B:CYS111 3.3 18.6 1.0
CB B:CYS100 3.4 24.0 1.0
CB B:CYS103 3.4 20.5 1.0
N B:CYS97 3.6 19.6 1.0
CB B:CYS97 3.6 21.7 1.0
N B:CYS100 3.8 30.6 1.0
CA B:CYS111 3.8 15.7 1.0
CA B:CYS97 4.0 21.7 1.0
N B:GLY98 4.0 26.2 1.0
N B:LEU112 4.0 15.6 1.0
CA B:CYS100 4.2 27.4 1.0
N B:CYS103 4.2 20.8 1.0
CA B:CYS103 4.4 21.9 1.0
C B:CYS97 4.4 23.5 1.0
C B:CYS111 4.4 16.4 1.0
N B:LYS99 4.5 30.7 1.0
C B:GLN96 4.6 18.5 1.0
C B:CYS100 4.8 27.4 1.0
O B:CYS100 4.8 28.9 1.0
C B:LYS99 4.9 32.5 1.0
CA B:GLN96 4.9 15.0 1.0
CA B:GLY98 4.9 26.8 1.0
N B:LYS113 5.0 18.5 1.0
CG B:LYS113 5.0 23.4 1.0

Reference:

S.Al-Karadaghi, E.S.Cedergren-Zeppezauer, Z.Dauter, K.S.Wilson. Refined Structure of Cu-Substituted Alcohol Dehydrogenase at 2.1 A Resolution. Acta Crystallogr.,Sect.D V. 51 805 1995.
ISSN: ISSN 0907-4449
PubMed: 15299812
DOI: 10.1107/S090744499500045X
Page generated: Wed Dec 16 03:47:23 2020

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