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Manganese in PDB 6h08: The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution

Enzymatic activity of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution

All present enzymatic activity of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution:
1.11.1.5;

Protein crystallography data

The structure of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution, PDB code: 6h08 was solved by M.Ortmayer, C.Levy, A.P.Green, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.86 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.920, 106.770, 163.720, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 20.5

Other elements in 6h08:

The structure of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution also contains other interesting chemical elements:

Cobalt (Co) 6 atoms
Iron (Fe) 3 atoms
Sodium (Na) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution (pdb code 6h08). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution, PDB code: 6h08:

Manganese binding site 1 out of 1 in 6h08

Go back to Manganese Binding Sites List in 6h08
Manganese binding site 1 out of 1 in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn303

b:40.7
occ:1.00
 O A:HOH564 2.0 50.9 1.0
NE2 A:HIS3 2.1 75.8 1.0
NE2 A:HIS1 2.2 45.0 1.0
O A:HOH441 2.2 46.6 1.0
CD2 A:HIS3 3.0 52.5 1.0
CD2 A:HIS1 3.1 53.4 1.0
CE1 A:HIS3 3.2 68.3 1.0
CE1 A:HIS1 3.2 55.1 1.0
CG A:HIS3 4.2 66.5 1.0
ND1 A:HIS3 4.2 72.8 1.0
CG A:HIS1 4.2 56.7 1.0
O A:HOH544 4.3 37.4 1.0
ND1 A:HIS1 4.3 52.5 1.0

Reference:

M.Ortmayer, K.Fisher, J.Basran, E.M.Wolde-Michael, D.J.Heyes, C.Levy, S.Lovelock, E.L.Raven, S.Hay, S.E.J.Rigby, A.P.Green. Rewiring the Push-Pull Catalytic Machinery of A Haem Enzyme Using An Expanded Genetic Code To Be Published.
Page generated: Tue Dec 15 04:54:04 2020

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