Molybdenum in PDB 3dmr: Structure of Dmso Reductase From Rhodobacter Capsulatus at pH 7.0

The structure of Structure of Dmso Reductase From Rhodobacter Capsulatus at pH 7.0, PDB code: 3dmr was solved by A.S.Mcalpine, S.Bailey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.450, 80.450, 229.110, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 24.2

The binding sites of Molybdenum atom in the Structure of Dmso Reductase From Rhodobacter Capsulatus at pH 7.0 (pdb code 3dmr). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Structure of Dmso Reductase From Rhodobacter Capsulatus at pH 7.0, PDB code: 3dmr:

Molybdenum binding site 1 out of 1 in the Structure of Dmso Reductase From Rhodobacter Capsulatus at pH 7.0


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Structure of Dmso Reductase From Rhodobacter Capsulatus at pH 7.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo784 b:12.2 occ:1.00 O A:O785 1.7 21.4 1.0 OG A:SER147 1.8 5.2 1.0 O A:O786 1.8 16.4 1.0 S12 A:PGD782 2.4 10.7 1.0 S12 A:PGD783 2.5 11.1 1.0 S13 A:PGD783 2.5 6.9 1.0 S13 A:PGD782 2.6 12.4 1.0 CB A:SER147 3.2 7.7 1.0 C12 A:PGD782 3.5 10.4 1.0 C13 A:PGD782 3.5 10.7 1.0 C13 A:PGD783 3.6 8.1 1.0 C12 A:PGD783 3.7 8.8 1.0 NE1 A:TRP116 3.9 7.3 1.0 CA A:SER147 3.9 9.3 1.0 N A:SER147 4.1 9.9 1.0 OH A:TYR114 4.2 11.5 1.0 O A:HOH1252 4.2 22.5 1.0 NE2 A:HIS649 4.4 4.6 1.0 CE1 A:HIS649 4.4 5.5 1.0 CE1 A:HIS643 4.6 13.2 1.0 CE2 A:TRP116 4.6 6.3 1.0 C A:TYR146 4.7 9.3 1.0 CZ2 A:TRP116 4.7 6.7 1.0 CD1 A:TRP116 4.8 7.0 1.0 C11 A:PGD782 5.0 9.8 1.0 C14 A:PGD782 5.0 10.6 1.0

A.S.Mcalpine, A.G.Mcewan, A.Shaw, S.Bailey. Molybdenum Active Centre of Dmso Reductase From Rhodobacter Capsulatus: Crystal Structure of the Oxidised Enzyme at 1.82-A Resolution and the Dithionite-Reduced Enzyme at 2.8-A Resolution J.Biol.Inorg.Chem. V. 2 690 1997.
ISSN: ISSN 0949-8257