Tungsten in PDB 1e18: Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus

The structure of Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus, PDB code: 1e18 was solved by S.Bailey, L.J.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.920, 80.920, 229.780, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 19.2

The binding sites of Tungsten atom in the Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus (pdb code 1e18). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total only one binding site of Tungsten was determined in the Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus, PDB code: 1e18:

Tungsten binding site 1 out of 1 in the Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Tungsten-Susbstituted Dmso Reductase From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ A:W803 b:13.4 occ:1.00 W A:6WO803 0.0 13.4 1.0 O1 A:6WO803 1.8 16.2 1.0 OG A:SER147 1.9 9.5 1.0 S13 A:PGD802 2.4 6.8 1.0 S12 A:PGD801 2.4 7.7 1.0 S12 A:PGD802 2.5 8.3 1.0 S13 A:PGD801 2.5 7.7 1.0 CB A:SER147 3.2 8.7 1.0 C13 A:PGD802 3.5 8.3 1.0 C13 A:PGD801 3.5 7.5 1.0 C12 A:PGD802 3.5 10.2 1.0 C12 A:PGD801 3.6 10.3 1.0 CA A:SER147 3.9 12.1 1.0 NE1 A:TRP116 3.9 15.1 1.0 N A:SER147 4.2 12.3 1.0 OH A:TYR114 4.3 20.5 1.0 CE1 A:HIS649 4.5 10.6 1.0 CE1 A:HIS643 4.6 12.6 1.0 NE2 A:HIS649 4.6 8.5 1.0 O A:HOH2103 4.6 54.0 1.0 CE2 A:TRP116 4.6 11.9 1.0 CZ2 A:TRP116 4.7 13.7 1.0 C A:TYR146 4.9 11.4 1.0 CD1 A:TRP116 4.9 11.9 1.0 C14 A:PGD802 4.9 10.5 1.0 C14 A:PGD801 4.9 11.9 1.0

L.J.Stewart, S.Bailey, B.Bennett, J.M.Charnock, C.D.Garner, A.S.Mcalpine. Dimethylsulfoxide Reductase: An Enzyme Capable of Catalysis with Either Molybdenum or Tungsten at the Active Site J.Mol.Biol. V. 299 593 2000.
ISSN: ISSN 0022-2836
PubMed: 10835270
DOI: 10.1006/JMBI.2000.3702