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Molybdenum in PDB 1n63: Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State

Enzymatic activity of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State

All present enzymatic activity of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State:
1.2.99.2;

Protein crystallography data

The structure of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State, PDB code: 1n63 was solved by H.Dobbek, L.Gremer, R.Kiefersauer, R.Huber, O.Meyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.00 / 1.21
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 118.962, 131.270, 159.648, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 18.5

Other elements in 1n63:

The structure of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State also contains other interesting chemical elements:

Iron (Fe) 8 atoms
Copper (Cu) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State (pdb code 1n63). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State, PDB code: 1n63:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1n63

Go back to Molybdenum Binding Sites List in 1n63
Molybdenum binding site 1 out of 2 in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo3921

b:11.1
occ:1.00
MO B:CUN3921 0.0 11.1 1.0
OM1 B:CUN3921 1.7 12.1 1.0
OM2 B:CUN3921 2.0 11.9 1.0
S B:CUN3921 2.3 11.6 1.0
S7' B:MCN3920 2.4 9.8 1.0
S8' B:MCN3920 2.4 9.6 1.0
OE2 B:GLU763 3.3 11.9 1.0
C7' B:MCN3920 3.3 10.6 1.0
C8' B:MCN3920 3.4 10.8 1.0
CU B:CUN3921 3.9 13.8 0.9
N B:GLY569 4.0 11.3 1.0
CA B:TYR568 4.0 12.1 1.0
CA B:GLY272 4.0 10.8 1.0
CD B:GLU763 4.0 10.7 1.0
N B:GLY272 4.0 10.4 1.0
CB B:TYR568 4.0 11.3 1.0
O B:HOH3969 4.1 11.4 1.0
O B:HOH4304 4.2 24.7 1.0
C B:PHE271 4.4 10.9 1.0
C B:TYR568 4.5 8.7 1.0
N B:ARG387 4.5 9.3 1.0
NE2 B:GLN240 4.6 11.3 1.0
CA B:ARG387 4.6 10.9 1.0
CG B:GLU763 4.6 12.3 1.0
OE1 B:GLU763 4.7 10.8 1.0
O B:PHE271 4.7 11.5 1.0
C6' B:MCN3920 4.8 10.6 1.0
C9' B:MCN3920 4.8 10.6 1.0

Molybdenum binding site 2 out of 2 in 1n63

Go back to Molybdenum Binding Sites List in 1n63
Molybdenum binding site 2 out of 2 in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Carbon Monoxide Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mo4921

b:11.7
occ:1.00
MO E:CUN4921 0.0 11.7 1.0
OM1 E:CUN4921 1.7 10.7 1.0
OM2 E:CUN4921 2.0 15.0 1.0
S E:CUN4921 2.3 12.8 1.0
S7' E:MCN4920 2.4 10.1 1.0
S8' E:MCN4920 2.4 10.4 1.0
OE2 E:GLU763 3.3 13.0 1.0
C7' E:MCN4920 3.3 10.3 1.0
C8' E:MCN4920 3.4 10.9 1.0
CU E:CUN4921 3.9 14.6 0.9
N E:GLY569 4.0 11.8 1.0
N E:GLY272 4.0 11.5 1.0
CD E:GLU763 4.0 11.3 1.0
CA E:TYR568 4.0 12.6 1.0
CA E:GLY272 4.0 12.0 1.0
CB E:TYR568 4.1 12.3 1.0
O E:HOH5295 4.1 33.3 1.0
O E:HOH4927 4.2 11.5 1.0
C E:PHE271 4.4 11.0 1.0
N E:ARG387 4.5 10.2 1.0
C E:TYR568 4.5 12.4 1.0
NE2 E:GLN240 4.6 10.9 1.0
CA E:ARG387 4.6 9.7 1.0
CG E:GLU763 4.6 11.2 1.0
O E:PHE271 4.7 11.6 1.0
OE1 E:GLU763 4.7 11.6 1.0
C6' E:MCN4920 4.8 10.3 1.0
C9' E:MCN4920 4.8 11.4 1.0

Reference:

H.Dobbek, L.Gremer, R.Kiefersauer, R.Huber, O.Meyer. Catalysis at A Dinuclear [Cusmo(=O)Oh] Cluster in A Co Dehydrogenase Resolved at 1.1-A Resolution Proc.Natl.Acad.Sci.Usa V. 99 15971 2002.
ISSN: ISSN 0027-8424
PubMed: 12475995
DOI: 10.1073/PNAS.212640899
Page generated: Tue Dec 15 05:16:14 2020

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