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Chlorine in PDB 4c7z: Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide

Enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide

All present enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide:
1.2.99.7;

Protein crystallography data

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide, PDB code: 4c7z was solved by H.D.Correia, M.J.Romao, T.Santos-Silva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 123.99 / 1.55
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 143.170, 143.170, 162.250, 90.00, 90.00, 120.00
R / Rfree (%) 13.49 / 15.627

Other elements in 4c7z:

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide also contains other interesting chemical elements:

Molybdenum (Mo) 1 atom
Magnesium (Mg) 3 atoms
Iron (Fe) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide (pdb code 4c7z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide, PDB code: 4c7z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4c7z

Go back to Chlorine Binding Sites List in 4c7z
Chlorine binding site 1 out of 2 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1913

b:15.2
occ:1.00
 O A:HOH2715 3.2 26.2 1.0
O A:HOH2638 3.2 25.4 1.0
N A:GLU899 3.3 11.3 1.0
CD A:PRO898 3.7 11.4 1.0
CB A:GLU899 3.8 11.5 1.0
N A:PRO898 3.8 10.7 1.0
CB A:TYR897 3.9 11.0 1.0
CA A:GLU899 4.1 11.5 1.0
CB A:PRO898 4.2 12.2 1.0
C A:PRO898 4.3 11.5 1.0
CG A:PRO898 4.3 12.6 1.0
CA A:PRO898 4.3 11.8 1.0
C A:TYR897 4.4 10.2 1.0
CA A:TYR897 4.6 10.1 1.0
CG A:TYR897 4.6 11.7 1.0
O A:HOH2657 4.8 37.6 1.0
O A:HOH2658 4.8 29.8 1.0
OE1 A:GLU899 4.9 13.7 1.0
CD1 A:TYR897 4.9 13.4 1.0

Chlorine binding site 2 out of 2 in 4c7z

Go back to Chlorine Binding Sites List in 4c7z
Chlorine binding site 2 out of 2 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Activated with Sodium Dithionite and Sodium Sulfide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1914

b:14.5
occ:1.00
 O A:HOH2708 3.0 24.5 1.0
O A:HOH2333 3.2 19.8 1.0
N A:TYR892 3.2 9.3 1.0
O A:HOH2710 3.3 25.7 1.0
N A:ARG893 3.4 9.5 1.0
CA A:TYR892 3.9 9.6 1.0
CG A:ARG893 3.9 10.3 1.0
CB A:ARG893 4.0 9.7 1.0
CB A:TYR892 4.0 9.7 1.0
CA A:ILE891 4.1 10.6 1.0
C A:ILE891 4.1 10.0 1.0
C A:TYR892 4.1 9.4 1.0
CG2 A:ILE891 4.1 10.9 1.0
CA A:ARG893 4.2 9.1 1.0
O A:ARG893 4.3 10.2 1.0
CD A:LYS900 4.3 12.8 1.0
CD2 A:TYR892 4.4 11.9 1.0
O A:HOH3210 4.5 21.0 1.0
CD A:ARG893 4.6 10.7 1.0
CD1 A:ILE891 4.6 13.2 1.0
CB A:ILE891 4.7 10.8 1.0
CG A:TYR892 4.7 10.7 1.0
C A:ARG893 4.7 9.6 1.0
CG A:LYS900 4.8 12.5 1.0
O A:ARG890 4.8 12.4 1.0
O A:HOH2719 4.9 39.3 1.0

Reference:

J.Marangon, H.D.Correia, C.D.Brondino, J.J.G.Moura, M.J.Romao, P.J.Gonzalez, T.Santos-Silva. Kinetic and Structural Studies of Aldehyde Oxidoreductase From Desulfovibrio Gigas Reveal A Dithiolene-Based Chemistry For Enzyme Activation and Inhibition By H2O2. Plos One V. 8 83234 2013.
ISSN: ISSN 1932-6203
PubMed: 24391748
DOI: 10.1371/JOURNAL.PONE.0083234
Page generated: Fri Jul 11 13:46:31 2025

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