Chlorine in PDB 3fc4: Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas

All present enzymatic activity of Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas:
1.2.99.7;

The structure of Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas, PDB code: 3fc4 was solved by T.Santos-Silva, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.44 / 1.79
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	142.800, 142.800, 161.550, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 18.9

The structure of Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas also contains other interesting chemical elements:

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

The binding sites of Chlorine atom in the Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas (pdb code 3fc4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas, PDB code: 3fc4:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl920 b:20.0 occ:1.00 O A:HOH1097 3.0 29.4 1.0 O A:HOH1117 3.1 30.1 1.0 O A:HOH1093 3.1 25.0 1.0 N A:GLU899 3.4 14.7 1.0 CD A:PRO898 3.6 15.3 1.0 CB A:GLU899 3.7 14.3 1.0 N A:PRO898 3.8 15.2 1.0 CB A:TYR897 3.9 15.8 1.0 CB A:PRO898 4.0 15.2 1.0 CA A:GLU899 4.1 14.9 1.0 CG A:PRO898 4.2 16.0 1.0 CA A:PRO898 4.3 14.5 1.0 C A:PRO898 4.3 15.1 1.0 C A:TYR897 4.3 14.7 1.0 CA A:TYR897 4.6 15.2 1.0 CG A:TYR897 4.6 16.3 1.0 O A:HOH1103 4.7 44.0 1.0 CD2 A:TYR897 4.9 16.5 1.0 O A:HOH1068 4.9 31.7 1.0 OE1 A:GLU899 4.9 16.7 1.0 O A:HOH2014 5.0 27.2 1.0

Chlorine binding site 2 out of 3 in the Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl916 b:27.3 occ:1.00 NH1 A:ARG460 3.4 10.4 1.0 NE2 A:GLN539 3.4 16.7 1.0 CA A:TYR535 3.5 14.0 1.0 O A:HOH1343 3.7 17.2 1.0 CG A:ARG460 3.7 14.2 1.0 N A:GLY536 3.7 13.6 1.0 N A:PHE532 3.8 12.8 1.0 O A:PHE532 3.8 13.6 1.0 CD1 A:LEU498 3.9 13.5 1.0 CD2 A:TYR535 4.1 11.1 1.0 N A:TYR535 4.1 13.7 1.0 C A:TYR535 4.1 13.9 1.0 CA A:ARG460 4.1 13.4 1.0 OE1 A:GLN539 4.2 12.8 1.0 N A:SER461 4.2 12.3 1.0 CD A:GLN539 4.3 15.5 1.0 CB A:PHE532 4.3 12.3 1.0 CB A:ARG460 4.3 13.0 1.0 CD2 A:LEU498 4.4 13.3 1.0 CB A:TYR535 4.4 13.8 1.0 CZ A:ARG460 4.5 12.4 1.0 CA A:PHE532 4.5 12.6 1.0 CD A:ARG460 4.6 13.3 1.0 C A:PHE532 4.6 12.3 1.0 C A:ALA531 4.6 13.3 1.0 CG A:TYR535 4.7 13.0 1.0 CA A:ALA531 4.7 13.4 1.0 O A:SER530 4.7 14.0 1.0 C A:ARG460 4.7 13.7 1.0 CG A:LEU498 4.8 12.7 1.0 CA A:GLY536 4.8 13.7 1.0 NE A:ARG460 4.9 12.3 1.0 CE2 A:TYR535 5.0 14.3 1.0

Chlorine binding site 3 out of 3 in the Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Ethylene Glycol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl918 b:21.8 occ:1.00 O A:HOH1867 2.9 41.1 1.0 N A:TYR892 3.2 15.4 1.0 O A:HOH985 3.2 23.8 1.0 O A:HOH934 3.3 30.0 1.0 N A:ARG893 3.3 15.0 1.0 CB A:ARG893 3.8 15.6 1.0 CA A:TYR892 3.9 15.2 1.0 CG A:ARG893 3.9 14.3 1.0 CB A:TYR892 4.0 15.4 1.0 C A:ILE891 4.1 15.6 1.0 CA A:ILE891 4.1 16.1 1.0 C A:TYR892 4.1 14.7 1.0 CG2 A:ILE891 4.1 16.4 1.0 CA A:ARG893 4.1 15.0 1.0 O A:ARG893 4.2 15.1 1.0 CD A:LYS900 4.3 17.7 1.0 CD2 A:TYR892 4.4 18.2 1.0 O A:HOH1641 4.5 28.2 1.0 CD A:ARG893 4.5 14.8 1.0 CB A:ILE891 4.7 16.2 1.0 C A:ARG893 4.7 14.9 1.0 CG A:LYS900 4.7 17.5 1.0 CD1 A:ILE891 4.7 21.4 1.0 O A:ARG890 4.7 16.2 1.0 CG A:TYR892 4.7 17.1 1.0 O A:HOH1030 4.8 41.2 1.0 O A:HOH1022 4.8 48.4 1.0 CE A:LYS900 4.9 21.1 1.0 O A:HOH1287 4.9 16.8 1.0 O A:HOH2073 4.9 49.3 1.0

T.Santos-Silva, F.Ferroni, A.Thapper, J.Marangon, P.J.Gonzalez, A.C.Rizzi, I.Moura, J.J.Moura, M.J.Romao, C.D.Brondino. Kinetic, Structural, and Epr Studies Reveal That Aldehyde Oxidoreductase From Desulfovibrio Gigas Does Not Need A Sulfido Ligand For Catalysis and Give Evidence For A Direct Mo-C Interaction in A Biological System. J.Am.Chem.Soc. V. 131 7990 2009.
ISSN: ISSN 0002-7863
PubMed: 19459677
DOI: 10.1021/JA809448R