Molybdenum in PDB 1dmr: Oxidized Dmso Reductase From Rhodobacter Capsulatus

The structure of Oxidized Dmso Reductase From Rhodobacter Capsulatus, PDB code: 1dmr 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 / 1.82
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.880, 80.880, 229.700, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 18.4

The binding sites of Molybdenum atom in the Oxidized Dmso Reductase From Rhodobacter Capsulatus (pdb code 1dmr). 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 Oxidized Dmso Reductase From Rhodobacter Capsulatus, PDB code: 1dmr:

Molybdenum binding site 1 out of 1 in the Oxidized Dmso Reductase From Rhodobacter Capsulatus


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Oxidized Dmso Reductase From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo784 b:12.7 occ:1.00 O A:O785 1.6 12.8 1.0 O A:O786 1.8 9.8 1.0 OG A:SER147 1.9 10.1 1.0 S13 A:PGD783 2.4 10.6 1.0 S13 A:PGD782 2.5 8.6 1.0 S12 A:PGD782 2.5 8.1 1.0 S12 A:PGD783 2.5 10.0 1.0 CB A:SER147 3.2 8.7 1.0 C13 A:PGD782 3.5 7.3 1.0 C12 A:PGD782 3.6 7.9 1.0 C13 A:PGD783 3.6 7.8 1.0 C12 A:PGD783 3.7 9.0 1.0 NE1 A:TRP116 3.9 12.8 1.0 CA A:SER147 3.9 7.6 1.0 N A:SER147 4.1 4.1 1.0 OH A:TYR114 4.2 16.9 1.0 O A:HOH974 4.2 36.6 1.0 CE1 A:HIS649 4.4 7.8 1.0 CE1 A:HIS643 4.5 8.4 1.0 NE2 A:HIS649 4.5 6.2 1.0 CE2 A:TRP116 4.6 11.3 1.0 CZ2 A:TRP116 4.7 10.2 1.0 C A:TYR146 4.8 5.9 1.0 CD1 A:TRP116 4.8 10.2 1.0 C14 A:PGD782 5.0 6.6 1.0 C14 A:PGD783 5.0 7.6 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