Molybdenum in PDB 8rqz: Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis

The structure of Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis, PDB code: 8rqz was solved by M.V.Cherrier, P.Arnoux, L.Martin, Y.Nicolet, G.Schoehn, P.Legrand, M.Broc, F.Seduk, G.Brasseur, R.Arias-Cartin, A.Magalon, A.Walburger, A.Uzel, B.Guigliarelli, S.Grimaldi, F.Pierrel, M.Mate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.41 / 2.69
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	210.833, 210.5, 494.213, 90, 90, 90
R / Rfree (%)	19.6 / 23.1

The structure of Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis also contains other interesting chemical elements:

Sodium	(Na)	1 atom
Iron	(Fe)	36 atoms

The binding sites of Molybdenum atom in the Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis (pdb code 8rqz). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis, PDB code: 8rqz:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo1008 b:49.3 occ:1.00 S13 C:MGD1007 2.4 42.0 1.0 S13 C:MGD1006 2.4 48.6 1.0 S C:H2S1010 2.4 41.7 0.6 SG C:CYS391 2.4 59.8 1.0 S12 C:MGD1007 2.4 42.0 1.0 S12 C:MGD1006 2.4 48.1 1.0 C12 C:MGD1006 3.3 48.0 1.0 CB C:CYS391 3.3 53.9 1.0 C12 C:MGD1007 3.3 42.2 1.0 C13 C:MGD1006 3.4 48.3 1.0 C13 C:MGD1007 3.4 41.9 1.0 CA C:GLY586 3.9 37.2 1.0 CA C:CYS391 4.4 52.1 1.0 O C:CYS387 4.5 50.7 1.0 N C:HIS587 4.5 36.5 1.0 NH1 C:ARG828 4.5 43.4 1.0 C C:GLY586 4.6 37.4 1.0 CD2 C:HIS587 4.6 35.9 1.0 C11 C:MGD1007 4.7 42.8 1.0 C11 C:MGD1006 4.7 47.7 1.0 N C:GLY586 4.8 36.6 1.0 NH2 C:ARG828 4.8 44.1 1.0 C14 C:MGD1007 4.8 41.6 1.0 C14 C:MGD1006 4.8 48.4 1.0 OE1 C:GLN392 4.8 63.1 1.0 CZ C:ARG828 5.0 44.8 1.0 NE2 C:HIS834 5.0 35.7 1.0

Molybdenum binding site 2 out of 2 in the Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Crystal Structure of Molybdenum Bispyranopterin Guanine Dinucleotide Formate Dehydrogenases FORCE1 From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ D:Mo1012 b:48.9 occ:1.00 SG D:CYS391 2.4 57.5 1.0 S D:H2S1014 2.4 33.9 0.6 S13 D:MGD1011 2.4 47.0 1.0 S13 D:MGD1010 2.4 51.5 1.0 S12 D:MGD1011 2.4 45.9 1.0 S12 D:MGD1010 2.4 49.7 1.0 CB D:CYS391 3.3 53.3 1.0 C12 D:MGD1011 3.3 46.7 1.0 C12 D:MGD1010 3.3 50.0 1.0 C13 D:MGD1011 3.4 46.8 1.0 C13 D:MGD1010 3.4 50.7 1.0 NH2 D:ARG828 3.9 43.6 1.0 CA D:GLY586 4.0 38.7 1.0 CA D:CYS391 4.4 52.1 1.0 N D:HIS587 4.5 37.5 1.0 O D:CYS387 4.6 52.3 1.0 NE2 D:GLN392 4.6 64.7 1.0 CD2 D:HIS587 4.6 36.4 1.0 C11 D:MGD1011 4.7 47.6 1.0 C D:GLY586 4.7 38.4 1.0 C11 D:MGD1010 4.8 49.6 1.0 C14 D:MGD1011 4.8 46.5 1.0 N D:GLY586 4.8 38.6 1.0 C14 D:MGD1010 4.9 50.7 1.0 CZ D:ARG828 4.9 44.4 1.0 NE2 D:HIS834 4.9 37.9 1.0 SD D:MET549 5.0 56.4 1.0 SG D:CYS387 5.0 50.4 1.0

M.V.Cherrier, P.Arnoux, L.Martin, Y.Nicolet, G.Schoehn, P.Legrand, M.Broc, F.Seduk, G.Brasseur, R.Arias-Cartin, A.Magalon, A.Walburger, A.Uzel, B.Guigliarelli, S.Grimaldi, F.Pierrel, M.Mate. Conserved Helical Membrane Plug-in For Quinone Reductases To Be Published.