Molybdenum in PDB 1h5n: Dmso Reductase Modified By the Presence of Dms and Air

All present enzymatic activity of Dmso Reductase Modified By the Presence of Dms and Air:
1.7.2.3; 1.8.5.3;

The structure of Dmso Reductase Modified By the Presence of Dms and Air, PDB code: 1h5n was solved by S.Bailey, B.Adams, A.T.Smith, R.L.Richards, D.J.Lowe, R.C.Bray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.800, 116.100, 230.400, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 20.9

The binding sites of Molybdenum atom in the Dmso Reductase Modified By the Presence of Dms and Air (pdb code 1h5n). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Dmso Reductase Modified By the Presence of Dms and Air, PDB code: 1h5n:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Dmso Reductase Modified By the Presence of Dms and Air


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Dmso Reductase Modified By the Presence of Dms and Air within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo1784 b:16.5 occ:1.00 OG A:SER147 1.8 24.9 1.0 S13 A:PGD1782 2.4 6.7 1.0 S13 A:PGD1783 2.4 8.3 1.0 S12 A:PGD1783 2.5 7.7 1.0 S12 A:PGD1782 2.5 7.5 1.0 CB A:SER147 2.6 29.9 1.0 CA A:SER147 3.1 33.4 1.0 C13 A:PGD1782 3.4 12.0 1.0 C13 A:PGD1783 3.5 10.2 1.0 C12 A:PGD1783 3.5 9.4 1.0 C12 A:PGD1782 3.5 12.1 1.0 N A:SER147 3.6 37.6 1.0 NE1 A:TRP116 4.0 11.5 1.0 CE1 A:HIS643 4.2 8.2 1.0 CE1 A:HIS649 4.3 11.8 1.0 OH A:TYR114 4.3 37.8 1.0 C A:TYR146 4.5 38.1 1.0 C A:SER147 4.5 34.0 1.0 NE2 A:HIS649 4.5 10.6 1.0 O A:HOH2172 4.7 52.1 1.0 CE2 A:TRP116 4.8 9.0 1.0 C14 A:PGD1783 4.9 8.8 1.0 C14 A:PGD1782 4.9 9.5 1.0 O A:TYR146 4.9 39.9 1.0 CD1 A:TRP116 4.9 11.7 1.0 CZ2 A:TRP116 4.9 8.7 1.0 O A:SER147 4.9 32.3 1.0 C11 A:PGD1783 5.0 8.7 1.0 NE2 A:HIS643 5.0 7.6 1.0

Molybdenum binding site 2 out of 2 in the Dmso Reductase Modified By the Presence of Dms and Air


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Dmso Reductase Modified By the Presence of Dms and Air within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo1784 b:16.9 occ:1.00 OG C:SER147 1.9 25.1 1.0 S13 C:PGD1782 2.4 7.2 1.0 S12 C:PGD1783 2.5 9.7 1.0 S13 C:PGD1783 2.5 9.3 1.0 S12 C:PGD1782 2.5 7.9 1.0 CB C:SER147 2.7 30.5 1.0 CA C:SER147 3.1 35.8 1.0 C13 C:PGD1782 3.4 8.6 1.0 C12 C:PGD1782 3.5 8.6 1.0 N C:SER147 3.5 38.4 1.0 C13 C:PGD1783 3.6 8.2 1.0 C12 C:PGD1783 3.6 8.1 1.0 NE1 C:TRP116 4.1 10.2 1.0 OH C:TYR114 4.2 40.0 1.0 CE1 C:HIS643 4.4 11.4 1.0 CE1 C:HIS649 4.4 11.5 1.0 C C:TYR146 4.4 38.9 1.0 O C:HOH2139 4.5 45.3 1.0 C C:SER147 4.5 35.5 1.0 NE2 C:HIS649 4.5 10.2 1.0 C14 C:PGD1782 4.8 7.8 1.0 CE2 C:TRP116 4.8 9.8 1.0 O C:TYR146 4.9 40.7 1.0 CD1 C:TRP116 4.9 12.1 1.0 CZ2 C:TRP116 5.0 7.0 1.0 C14 C:PGD1783 5.0 11.0 1.0 O C:SER147 5.0 35.6 1.0 C11 C:PGD1782 5.0 9.3 1.0

R.C.Bray, B.Adams, A.T.Smith, R.L.Richards, D.J.Lowe, S.Bailey. Reactions of Dimethyl Sulphoxide Reductase in the Presence of Dimethylsulphide and the Structure of the Dimethylsulphide-Modified Enzyme Biochemistry V. 40 9810 2001.
ISSN: ISSN 0006-2960
PubMed: 11502174
DOI: 10.1021/BI010559R