Molybdenum in PDB 1dms: Structure of Dmso Reductase

The structure of Structure of Dmso Reductase, PDB code: 1dms was solved by F.Schneider, J.Loewe, R.Huber, H.Schindelin, C.Kisker, J.Knaeblein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.88
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.700, 80.700, 229.200, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 20.3

The binding sites of Molybdenum atom in the Structure of Dmso Reductase (pdb code 1dms). 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, PDB code: 1dms:

Molybdenum binding site 1 out of 1 in the Structure of Dmso Reductase


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo784 b:21.8 occ:1.00 MO A:2MO784 0.0 21.8 1.0 OT1 A:2MO784 1.7 22.8 1.0 OT2 A:2MO784 1.7 24.2 1.0 OG A:SER147 2.0 8.8 1.0 S12 A:PGD782 2.3 8.3 1.0 S13 A:PGD782 2.6 7.4 1.0 CB A:SER147 3.1 8.1 1.0 C12 A:PGD782 3.3 7.3 1.0 N A:SER147 3.3 8.1 1.0 C13 A:PGD782 3.3 7.2 1.0 S13 A:PGD783 3.5 10.4 1.0 OH A:TYR114 3.5 19.3 1.0 CA A:SER147 3.5 7.9 1.0 S12 A:PGD783 3.9 9.6 1.0 NE1 A:TRP116 4.0 8.7 1.0 C A:TYR146 4.0 7.9 1.0 N A:TYR146 4.4 7.5 1.0 CB A:TYR146 4.4 7.3 1.0 CZ A:TYR114 4.5 17.0 1.0 CA A:TYR146 4.5 7.6 1.0 O A:HOH1021 4.7 28.2 1.0 CE2 A:TYR114 4.7 16.6 1.0 CD1 A:TRP116 4.7 8.1 1.0 OD1 A:ASP145 4.7 8.2 1.0 C11 A:PGD782 4.7 6.9 1.0 C14 A:PGD782 4.7 6.7 1.0 O A:TYR146 4.8 7.8 1.0 NE2 A:HIS649 4.8 5.2 1.0 CE1 A:HIS649 4.9 5.2 1.0 CB A:ASP145 4.9 7.9 1.0 CG A:ASP145 4.9 8.4 1.0

F.Schneider, J.Lowe, R.Huber, H.Schindelin, C.Kisker, J.Knablein. Crystal Structure of Dimethyl Sulfoxide Reductase From Rhodobacter Capsulatus at 1.88 A Resolution. J.Mol.Biol. V. 263 53 1996.
ISSN: ISSN 0022-2836
PubMed: 8890912
DOI: 10.1006/JMBI.1996.0555