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Manganese in PDB 2i0k: Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant

Enzymatic activity of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant

All present enzymatic activity of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant:
1.1.3.6;

Protein crystallography data

The structure of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant, PDB code: 2i0k was solved by A.Vrielink, L.Lim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.55 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 140.635, 85.851, 78.755, 90.00, 112.48, 90.00
R / Rfree (%) 14.8 / 16.7

Other elements in 2i0k:

The structure of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant also contains other interesting chemical elements:

Arsenic (As) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant (pdb code 2i0k). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant, PDB code: 2i0k:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2i0k

Go back to Manganese Binding Sites List in 2i0k
Manganese binding site 1 out of 2 in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:11.3
occ:1.00
O2 A:CAC703 2.1 14.2 1.0
O A:HOH1135 2.1 17.7 1.0
O A:HOH1250 2.2 15.8 1.0
OD1 A:ASN542 2.2 8.6 1.0
OE2 A:GLU579 2.3 12.6 1.0
O A:HOH1074 2.3 11.6 1.0
CD A:GLU579 3.2 10.7 1.0
CG A:ASN542 3.3 7.9 1.0
OE1 A:GLU579 3.4 12.1 1.0
AS A:CAC703 3.5 15.6 1.0
ND2 A:ASN542 4.0 9.9 1.0
C1 A:CAC703 4.0 14.3 1.0
O A:HOH1068 4.1 14.2 1.0
O A:HOH2030 4.2 20.5 1.0
O A:HOH2437 4.2 31.2 1.0
O A:HOH1060 4.2 13.4 1.0
O A:HOH1155 4.3 17.6 1.0
O A:HOH1105 4.4 12.7 1.0
O A:HOH2419 4.4 27.3 1.0
O1 A:CAC703 4.5 12.6 1.0
CB A:ASN542 4.5 7.5 1.0
CG A:GLU579 4.5 9.5 1.0
OG1 A:THR547 4.6 9.3 1.0
CA A:ASN542 4.7 7.6 1.0
O A:HOH2331 4.9 27.5 1.0
C A:ASN542 5.0 7.8 1.0
C2 A:CAC703 5.0 14.1 1.0

Manganese binding site 2 out of 2 in 2i0k

Go back to Manganese Binding Sites List in 2i0k
Manganese binding site 2 out of 2 in the Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Cholesterol Oxidase From Brevibacterium Sterolicum- HIS121ALA Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn702

b:27.0
occ:1.00
O A:HOH2401 2.0 17.7 1.0
OD1 A:ASP545 2.1 13.7 1.0
O A:HOH2400 2.1 29.1 1.0
OD1 A:ASP544 2.2 13.8 0.5
O A:HOH2402 2.3 31.3 1.0
CG A:ASP545 3.1 12.3 1.0
CG A:ASP544 3.1 12.8 0.5
OD2 A:ASP544 3.3 18.2 0.5
OD2 A:ASP545 3.5 12.9 1.0
OD2 A:ASP544 4.1 14.2 0.5
CB A:ASP544 4.3 10.2 0.5
CB A:ASP545 4.3 9.8 1.0
O A:HOH1176 4.4 18.6 1.0
C A:ASP544 4.4 10.0 1.0
O A:HOH2561 4.4 37.5 1.0
O A:ASP544 4.5 10.8 1.0
N A:ASP545 4.5 9.6 1.0
CB A:ASP544 4.5 10.6 0.5
O A:HOH2353 4.5 24.9 1.0
CA A:ASP545 4.6 9.5 1.0
O A:HOH1133 4.6 14.9 1.0
CG A:ASP544 4.6 11.1 0.5
O A:HOH2312 4.7 22.9 1.0

Reference:

L.Lim, G.Molla, N.Guinn, S.Ghisla, L.Pollegioni, A.Vrielink. Structural and Kinetic Analyses of the H121A Mutant of Cholesterol Oxidase. Biochem.J. V. 400 13 2006.
ISSN: ISSN 0264-6021
PubMed: 16856877
DOI: 10.1042/BJ20060664
Page generated: Tue Dec 15 04:02:38 2020

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