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Molybdenum in PDB 1zxi: Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans

Enzymatic activity of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans

All present enzymatic activity of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans:
1.2.99.2;

Protein crystallography data

The structure of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans, PDB code: 1zxi was solved by M.Resch, H.Dobbek, O.Meyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 118.840, 131.320, 159.990, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19.4

Other elements in 1zxi:

The structure of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans also contains other interesting chemical elements:

Iron (Fe) 8 atoms
Copper (Cu) 4 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans (pdb code 1zxi). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans, PDB code: 1zxi:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1zxi

Go back to Molybdenum Binding Sites List in 1zxi
Molybdenum binding site 1 out of 2 in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo3920

b:13.0
occ:1.00
MO B:CUM3920 0.0 13.0 1.0
OM1 B:CUM3920 1.7 16.0 1.0
OM2 B:CUM3920 1.8 15.3 1.0
S B:CUM3920 2.2 17.0 0.8
S7' B:MCN3921 2.4 12.8 1.0
S8' B:MCN3921 2.5 13.3 1.0
OE2 B:GLU763 3.2 16.4 1.0
C7' B:MCN3921 3.4 11.5 1.0
C8' B:MCN3921 3.5 14.8 1.0
CU B:CU3910 3.5 14.7 0.2
CU B:CUM3920 3.8 15.7 0.6
N B:GLY569 3.9 12.1 1.0
CA B:TYR568 3.9 12.6 1.0
CA B:GLY272 4.0 10.8 1.0
N B:GLY272 4.0 12.5 1.0
CD B:GLU763 4.0 13.3 1.0
CB B:TYR568 4.0 13.4 1.0
O B:HOH3968 4.2 11.3 1.0
N B:ARG387 4.3 12.6 1.0
C B:PHE271 4.3 11.5 1.0
C B:TYR568 4.4 12.0 1.0
CA B:ARG387 4.4 12.3 1.0
NE2 B:GLN240 4.6 9.8 1.0
CG B:GLU763 4.6 13.1 1.0
O B:PHE271 4.6 12.3 1.0
OE1 B:GLU763 4.8 14.9 1.0
C6' B:MCN3921 4.9 9.7 1.0
C9' B:MCN3921 4.9 11.6 1.0
CA B:GLY569 4.9 12.2 1.0
CA B:PHE271 5.0 11.0 1.0

Molybdenum binding site 2 out of 2 in 1zxi

Go back to Molybdenum Binding Sites List in 1zxi
Molybdenum binding site 2 out of 2 in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mo3922

b:14.8
occ:1.00
MO E:CUM3922 0.0 14.8 1.0
OM1 E:CUM3922 1.7 16.3 1.0
OM2 E:CUM3922 1.8 14.7 1.0
S E:CUM3922 2.2 16.7 0.8
S7' E:MCN3923 2.4 13.2 1.0
S8' E:MCN3923 2.5 13.0 1.0
OE2 E:GLU763 3.3 14.7 1.0
CU E:CU3911 3.3 15.0 0.2
C7' E:MCN3923 3.4 13.4 1.0
C8' E:MCN3923 3.5 13.8 1.0
CU E:CUM3922 3.8 17.3 0.6
N E:GLY569 3.9 11.1 1.0
CA E:GLY272 3.9 11.8 1.0
N E:GLY272 3.9 12.4 1.0
CA E:TYR568 4.0 12.0 1.0
CD E:GLU763 4.0 13.1 1.0
CB E:TYR568 4.1 12.8 1.0
O E:HOH3929 4.1 11.4 1.0
C E:PHE271 4.3 12.4 1.0
N E:ARG387 4.3 12.1 1.0
CA E:ARG387 4.5 13.2 1.0
C E:TYR568 4.5 11.9 1.0
O E:PHE271 4.6 10.9 1.0
NE2 E:GLN240 4.7 9.6 1.0
CG E:GLU763 4.7 12.8 1.0
OE1 E:GLU763 4.8 12.3 1.0
C6' E:MCN3923 4.9 11.4 1.0
C9' E:MCN3923 4.9 12.8 1.0
CA E:GLY569 4.9 11.5 1.0
CA E:PHE271 5.0 10.7 1.0

Reference:

M.Resch, H.Dobbek, O.Meyer. Structural and Functional Reconstruction in Situ of the [Cusmoo(2)] Active Site of Carbon Monoxide Dehydrogenase From the Carbon Monoxide Oxidizing Eubacterium Oligotropha Carboxidovorans J.Biol.Inorg.Chem. V. 10 518 2005.
ISSN: ISSN 0949-8257
PubMed: 16091936
DOI: 10.1007/S00775-005-0006-4
Page generated: Tue Dec 15 05:16:49 2020

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