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Molybdenum in PDB 1v97: Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form

Enzymatic activity of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form

All present enzymatic activity of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form:
1.1.1.204;

Protein crystallography data

The structure of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form, PDB code: 1v97 was solved by K.Okamoto, K.Matsumoto, R.Hille, B.T.Eger, E.F.Pai, T.Nishino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.94
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 167.987, 124.612, 146.926, 90.00, 90.99, 90.00
R / Rfree (%) 17.8 / 20.8

Other elements in 1v97:

The structure of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form also contains other interesting chemical elements:

Iron (Fe) 8 atoms
Calcium (Ca) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form (pdb code 1v97). 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 Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form, PDB code: 1v97:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1v97

Go back to Molybdenum Binding Sites List in 1v97
Molybdenum binding site 1 out of 2 in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form


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 Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo3004

b:14.4
occ:1.00
MO A:MOS3004 0.0 14.4 1.0
O2 A:MOS3004 1.7 12.8 1.0
O1 A:MOS3004 2.1 16.6 1.0
S2' A:MTE3003 2.4 12.6 1.0
S A:MOS3004 2.4 15.8 1.0
S1' A:MTE3003 2.4 10.2 1.0
C1' A:MTE3003 3.2 12.8 1.0
CPR A:FYX3006 3.3 16.0 1.0
C2' A:MTE3003 3.3 11.9 1.0
NPS A:FYX3006 3.9 17.4 1.0
OE2 A:GLU1261 3.9 12.7 1.0
CA A:GLY799 3.9 11.5 1.0
CB A:ALA1078 4.0 15.9 1.0
N A:GLY799 4.1 9.8 1.0
CD A:GLU1261 4.1 10.3 1.0
N A:ALA1079 4.2 12.1 1.0
CA A:ALA1078 4.4 12.1 1.0
CPO A:FYX3006 4.4 16.7 1.0
C A:PHE798 4.5 10.8 1.0
C6 A:MTE3003 4.5 11.2 1.0
NE2 A:GLN767 4.6 10.1 1.0
CG A:GLU1261 4.6 9.8 1.0
OE1 A:GLU1261 4.6 10.9 1.0
CA A:ARG912 4.7 11.9 1.0
N A:ARG912 4.7 12.2 1.0
O A:PHE798 4.8 11.9 1.0
C3' A:MTE3003 4.8 12.7 1.0
C A:ALA1078 4.8 13.9 1.0
OE2 A:GLU802 4.9 13.8 1.0

Molybdenum binding site 2 out of 2 in 1v97

Go back to Molybdenum Binding Sites List in 1v97
Molybdenum binding site 2 out of 2 in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form


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 Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo4004

b:14.5
occ:1.00
MO B:MOS4004 0.0 14.5 1.0
O2 B:MOS4004 1.7 10.8 1.0
O1 B:MOS4004 2.0 15.9 1.0
S2' B:MTE4003 2.4 12.7 1.0
S B:MOS4004 2.4 13.6 1.0
S1' B:MTE4003 2.4 9.2 1.0
C1' B:MTE4003 3.2 11.2 1.0
CPR B:FYX4006 3.2 17.6 1.0
C2' B:MTE4003 3.3 12.9 1.0
NPS B:FYX4006 3.8 19.4 1.0
OE2 B:GLU1261 3.9 12.4 1.0
CA B:GLY799 4.0 9.5 1.0
CB B:ALA1078 4.0 13.7 1.0
N B:GLY799 4.1 11.4 1.0
CD B:GLU1261 4.1 12.7 1.0
N B:ALA1079 4.2 13.1 1.0
CPO B:FYX4006 4.4 15.5 1.0
CA B:ALA1078 4.4 11.8 1.0
C B:PHE798 4.5 10.9 1.0
CG B:GLU1261 4.5 9.4 1.0
OE1 B:GLU1261 4.6 12.7 1.0
C6 B:MTE4003 4.6 11.7 1.0
NE2 B:GLN767 4.6 12.4 1.0
CA B:ARG912 4.7 11.5 1.0
N B:ARG912 4.7 11.4 1.0
O B:PHE798 4.7 12.3 1.0
C B:ALA1078 4.8 13.3 1.0
C3' B:MTE4003 4.8 13.4 1.0
OE2 B:GLU802 4.8 14.3 1.0

Reference:

K.Okamoto, K.Matsumoto, R.Hille, B.T.Eger, E.F.Pai, T.Nishino. The Crystal Structure of Xanthine Oxidoreductase During Catalysis: Implications For Reaction Mechanism and Enzyme Inhibition. Proc.Natl.Acad.Sci.Usa V. 101 7931 2004.
ISSN: ISSN 0027-8424
PubMed: 15148401
DOI: 10.1073/PNAS.0400973101
Page generated: Tue Dec 15 05:16:38 2020

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