Zinc in PDB 8eiy: Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide

Enzymatic activity of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide

All present enzymatic activity of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide:
1.1.1.1;

Protein crystallography data

The structure of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide, PDB code: 8eiy was solved by C.Zheng, I.I.Mathews, S.G.Boxer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.09 / 2.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.1, 71.54, 92.44, 90, 102.95, 90
R / Rfree (%) 20.8 / 26.3

Other elements in 8eiy:

The structure of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide (pdb code 8eiy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide, PDB code: 8eiy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8eiy

Go back to Zinc Binding Sites List in 8eiy
Zinc binding site 1 out of 2 in the Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:53.2
occ:1.00
 SG A:CYS100 2.3 64.2 1.0
SG A:CYS111 2.3 58.5 1.0
SG A:CYS97 2.3 59.7 1.0
SG A:CYS103 2.3 53.5 1.0
CB A:CYS111 3.2 56.8 1.0
CB A:CYS103 3.3 56.6 1.0
CB A:CYS100 3.4 57.3 1.0
N A:CYS97 3.4 55.0 1.0
CB A:CYS97 3.6 51.0 1.0
CA A:CYS111 3.8 55.5 1.0
N A:GLY98 3.9 56.8 1.0
N A:LEU112 4.0 61.1 1.0
CA A:CYS97 4.0 53.1 1.0
N A:CYS100 4.2 57.8 1.0
N A:CYS103 4.2 62.5 1.0
CA A:CYS103 4.4 60.2 1.0
C A:CYS111 4.4 58.9 1.0
C A:CYS97 4.4 52.4 1.0
CA A:CYS100 4.4 60.3 1.0
C A:GLN96 4.4 59.3 1.0
CA A:GLN96 4.6 53.0 1.0
CD1 A:LEU112 4.7 66.6 1.0
N A:LYS99 4.7 55.6 1.0
CA A:GLY98 4.9 57.0 1.0

Zinc binding site 2 out of 2 in 8eiy

Go back to Zinc Binding Sites List in 8eiy
Zinc binding site 2 out of 2 in the Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:55.8
occ:1.00
 SG B:CYS103 2.3 57.0 1.0
SG B:CYS111 2.3 60.1 1.0
SG B:CYS100 2.3 52.7 1.0
SG B:CYS97 2.3 60.1 1.0
CB B:CYS103 3.3 66.5 1.0
CB B:CYS111 3.3 49.1 1.0
CB B:CYS97 3.4 60.4 1.0
N B:CYS97 3.5 55.5 1.0
CB B:CYS100 3.6 52.2 1.0
N B:GLY98 3.7 65.8 1.0
N B:CYS100 3.8 56.9 1.0
CA B:CYS97 3.9 60.8 1.0
CA B:CYS111 4.0 54.4 1.0
N B:CYS103 4.1 64.2 1.0
C B:CYS97 4.2 65.3 1.0
CA B:CYS103 4.2 68.1 1.0
CA B:CYS100 4.2 61.8 1.0
N B:LYS99 4.3 60.8 1.0
N B:LEU112 4.3 49.3 1.0
C B:GLN96 4.5 59.5 1.0
C B:CYS111 4.6 51.8 1.0
CA B:GLY98 4.6 61.0 1.0
CA B:GLN96 4.8 54.5 1.0
N B:LYS113 4.8 46.9 1.0
C B:GLY98 4.9 56.3 1.0
CG B:LYS113 4.9 60.4 1.0
C B:LYS99 4.9 62.7 1.0
C B:CYS100 4.9 60.6 1.0

Reference:

C.Zheng, I.I.Mathews, S.G.Boxer. Structure of Cobalt(II)-Substituted S48T Horse Liver Alcohol Dehydrogenase at 2.55 Angstroms Resolution To Be Published.
Page generated: Wed Oct 30 19:52:02 2024

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