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Molybdenum in PDB 1e60: Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer

Enzymatic activity of Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer

All present enzymatic activity of Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer:
1.7.2.3; 1.8.5.3;

Protein crystallography data

The structure of Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer, PDB code: 1e60 was solved by S.Bailey, B.Bennett, B.Adams, A.T.Smith, 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 (°) 68.553, 115.920, 229.649, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.1

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer (pdb code 1e60). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer, PDB code: 1e60:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1e60

Go back to Molybdenum Binding Sites List in 1e60
Molybdenum binding site 1 out of 2 in the Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer


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 Exposed to Hepes - Structure II Buffer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo803

b:25.8
occ:1.00
MO A:2MO803 0.0 25.8 1.0
OT1 A:2MO803 1.8 21.2 1.0
OT2 A:2MO803 1.8 19.8 1.0
OG A:SER147 1.9 17.9 1.0
S12 A:PGD801 2.3 9.0 1.0
S13 A:PGD801 2.6 7.6 1.0
OH A:TYR114 2.9 32.1 1.0
CB A:SER147 3.0 13.2 1.0
N A:SER147 3.3 10.3 1.0
C12 A:PGD801 3.3 9.7 1.0
C13 A:PGD801 3.3 9.1 1.0
S13 A:PGD802 3.4 10.6 1.0
CA A:SER147 3.5 11.3 1.0
NE1 A:TRP116 3.9 12.3 1.0
C A:TYR146 4.0 9.0 1.0
S12 A:PGD802 4.1 12.1 1.0
O A:HOH2682 4.1 49.1 1.0
CZ A:TYR114 4.2 28.6 1.0
N A:TYR146 4.3 8.8 1.0
CB A:TYR146 4.3 8.1 1.0
CA A:TYR146 4.4 8.2 1.0
CE2 A:TYR114 4.5 26.9 1.0
CD1 A:TRP116 4.6 11.6 1.0
OD1 A:ASP145 4.7 12.2 1.0
O A:TYR146 4.7 10.7 1.0
C11 A:PGD801 4.7 8.9 1.0
CB A:ASP145 4.8 9.6 1.0
C14 A:PGD801 4.8 8.3 1.0
CG A:ASP145 4.9 12.3 1.0
CE1 A:HIS649 4.9 13.8 1.0
C A:SER147 4.9 11.6 1.0
NE2 A:HIS649 5.0 12.9 1.0
CE2 A:TRP116 5.0 10.3 1.0
C13 A:PGD802 5.0 10.4 1.0

Molybdenum binding site 2 out of 2 in 1e60

Go back to Molybdenum Binding Sites List in 1e60
Molybdenum binding site 2 out of 2 in the Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Oxidized Dmso Reductase Exposed to Hepes - Structure II Buffer within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo803

b:28.3
occ:1.00
MO C:2MO803 0.0 28.3 1.0
OT2 C:2MO803 1.8 25.2 1.0
OT1 C:2MO803 1.8 34.2 1.0
OG C:SER147 1.9 19.4 1.0
S12 C:PGD801 2.3 9.2 1.0
S13 C:PGD801 2.6 10.4 1.0
CB C:SER147 3.0 14.3 1.0
OH C:TYR114 3.0 29.1 1.0
N C:SER147 3.3 11.2 1.0
C12 C:PGD801 3.3 10.3 1.0
C13 C:PGD801 3.4 10.0 1.0
S13 C:PGD802 3.4 16.0 1.0
CA C:SER147 3.5 12.8 1.0
NE1 C:TRP116 3.9 12.5 1.0
C C:TYR146 4.0 10.8 1.0
S12 C:PGD802 4.1 15.9 1.0
CZ C:TYR114 4.2 25.6 1.0
N C:TYR146 4.3 12.1 1.0
CB C:TYR146 4.3 11.4 1.0
CA C:TYR146 4.5 11.0 1.0
OD1 C:ASP145 4.6 11.2 1.0
CE2 C:TYR114 4.6 24.2 1.0
CD1 C:TRP116 4.6 10.8 1.0
C11 C:PGD801 4.7 9.3 1.0
O C:TYR146 4.8 10.4 1.0
C14 C:PGD801 4.8 9.5 1.0
O C:HOH2628 4.8 49.8 1.0
CB C:ASP145 4.9 12.2 1.0
NE2 C:HIS649 4.9 12.7 1.0
CE1 C:HIS649 4.9 13.6 1.0
CG C:ASP145 4.9 12.8 1.0
C C:SER147 4.9 12.2 1.0
CE2 C:TRP116 5.0 11.8 1.0
C13 C:PGD802 5.0 13.2 1.0

Reference:

R.C.Bray, B.Adams, A.T.Smith, B.Bennett, S.Bailey. Reversible Dissociation of Thiolate Ligands From Molybdenum in An Enzyme of the Dimethyl Sulfoxide Reductase Family Biochemistry V. 39 11258 2000.
ISSN: ISSN 0006-2960
PubMed: 10985771
DOI: 10.1021/BI0000521
Page generated: Tue Dec 15 05:15:18 2020

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