Chlorine in PDB 6yu9: Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution

Enzymatic activity of Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution

All present enzymatic activity of Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution:
1.2.99.2;

Protein crystallography data

The structure of Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution, PDB code: 6yu9 was solved by T.Wagner, O.N.Lemaire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.75 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 106.531, 109.446, 129.280, 90.00, 112.55, 90.00
R / Rfree (%) 15.8 / 20.3

Other elements in 6yu9:

The structure of Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution also contains other interesting chemical elements:

Nickel (Ni) 4 atoms
Iron (Fe) 40 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution (pdb code 6yu9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution, PDB code: 6yu9:

Chlorine binding site 1 out of 1 in 6yu9

Go back to Chlorine Binding Sites List in 6yu9
Chlorine binding site 1 out of 1 in the Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Co-Dehydrogenase Homodimer From Clostridium Autoethanogenum at 1.90-A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl704

b:63.4
occ:1.00
 O C:HOH935 3.0 43.9 1.0
NZ C:LYS628 3.1 67.4 1.0
CB C:GLU624 3.4 44.9 1.0
OE2 C:GLU624 3.4 84.6 1.0
NH1 C:ARG621 3.6 24.5 1.0
CG C:LYS625 4.0 40.9 1.0
CZ C:ARG621 4.0 31.8 1.0
CD C:ARG621 4.1 27.7 1.0
N C:LYS625 4.1 40.1 1.0
C C:GLU624 4.2 39.4 1.0
NE C:ARG621 4.2 27.5 1.0
CD C:GLU624 4.3 77.9 1.0
CE C:LYS628 4.3 64.0 1.0
CG C:GLU624 4.3 59.3 1.0
CA C:GLU624 4.5 38.6 1.0
O C:ARG621 4.6 27.5 1.0
CA C:LYS625 4.6 39.3 1.0
O C:GLU624 4.6 40.3 1.0
CE C:LYS625 4.6 47.0 1.0
NH2 C:ARG621 4.9 36.1 1.0
O C:HOH828 4.9 23.5 1.0
CB C:LYS625 4.9 38.9 1.0
CD C:LYS625 5.0 43.2 1.0
OE2 C:GLU598 5.0 45.0 1.0

Reference:

O.N.Lemaire, T.Wagner. Gas Channel Rerouting in A Primordial Enzyme: Structural Insights of the Carbon-Monoxide Dehydrogenase/Acetyl-Coa Synthase Complex From the Acetogen Clostridium Autoethanogenum. Biochim Biophys Acta V.1862 48330 2020BIOENERG.
ISSN: ISSN 1879-2650
PubMed: 33080205
DOI: 10.1016/J.BBABIO.2020.148330
Page generated: Sat Dec 12 14:44:30 2020

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