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Iron 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
Manganese (Mn) 1 atom
Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron 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 Iron atom.
In total 3 binding sites of Iron where determined in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with A HIS175ME-His Proximal Ligand Substitution, PDB code: 6h08:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 6h08

Go back to Iron Binding Sites List in 6h08
Iron binding site 1 out of 3 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 Iron with other atoms in the Fe 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:Fe301

b:22.9
occ:1.00
FE A:HEM301 0.0 22.9 1.0
ND A:HEM301 1.9 24.6 1.0
NA A:HEM301 2.0 24.3 1.0
NB A:HEM301 2.1 24.3 1.0
NC A:HEM301 2.1 23.8 1.0
NE2 A:MHS175 2.1 24.9 1.0
O A:HOH459 2.4 44.7 1.0
C4D A:HEM301 2.9 23.7 1.0
C1D A:HEM301 2.9 21.6 1.0
C1A A:HEM301 3.0 23.7 1.0
C4A A:HEM301 3.0 26.0 1.0
C4B A:HEM301 3.0 25.8 1.0
C1B A:HEM301 3.1 23.6 1.0
CE1 A:MHS175 3.1 23.9 1.0
C4C A:HEM301 3.1 21.8 1.0
C1C A:HEM301 3.1 22.6 1.0
CD2 A:MHS175 3.1 25.9 1.0
CHA A:HEM301 3.4 22.2 1.0
CHD A:HEM301 3.4 22.7 1.0
CHC A:HEM301 3.4 22.5 1.0
CHB A:HEM301 3.4 25.4 1.0
NE1 A:TRP51 4.0 21.6 1.0
NE A:ARG48 4.1 18.6 0.5
O A:HOH537 4.1 34.9 1.0
C2D A:HEM301 4.2 20.9 1.0
C2A A:HEM301 4.2 23.6 1.0
ND1 A:MHS175 4.2 25.1 1.0
C3D A:HEM301 4.2 21.2 1.0
C3A A:HEM301 4.2 25.8 1.0
C2C A:HEM301 4.3 21.9 1.0
CG A:MHS175 4.3 23.8 1.0
C2B A:HEM301 4.3 24.2 1.0
C3C A:HEM301 4.3 22.1 1.0
C3B A:HEM301 4.3 23.4 1.0
CD1 A:TRP51 4.6 23.5 1.0
NH1 A:ARG48 4.6 12.8 0.5
CZ A:ARG48 4.9 16.9 0.5
CH2 A:TRP191 4.9 23.6 1.0
CD A:ARG48 4.9 19.7 0.5

Iron binding site 2 out of 3 in 6h08

Go back to Iron Binding Sites List in 6h08
Iron binding site 2 out of 3 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 Iron with other atoms in the Fe binding site number 2 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
B:Fe302

b:24.0
occ:1.00
FE B:HEM302 0.0 24.0 1.0
ND B:HEM302 1.9 23.4 1.0
NA B:HEM302 2.0 23.0 1.0
NC B:HEM302 2.1 22.8 1.0
NB B:HEM302 2.1 23.8 1.0
NE2 B:MHS175 2.2 25.6 1.0
O B:HOH470 2.3 46.3 1.0
C4D B:HEM302 2.9 24.3 1.0
C1D B:HEM302 2.9 21.3 1.0
C1A B:HEM302 3.0 27.1 1.0
C4A B:HEM302 3.0 24.1 1.0
C4B B:HEM302 3.0 23.4 1.0
C4C B:HEM302 3.1 19.6 1.0
C1B B:HEM302 3.1 22.3 1.0
C1C B:HEM302 3.1 25.8 1.0
CE1 B:MHS175 3.1 25.6 1.0
CD2 B:MHS175 3.2 24.9 1.0
CHA B:HEM302 3.4 21.0 1.0
CHD B:HEM302 3.4 21.0 1.0
CHB B:HEM302 3.4 26.2 1.0
CHC B:HEM302 3.4 23.6 1.0
NE1 B:TRP51 4.0 20.8 1.0
NE B:ARG48 4.1 18.8 0.5
O B:HOH501 4.2 35.8 1.0
C2A B:HEM302 4.2 27.3 1.0
C2D B:HEM302 4.2 22.1 1.0
C3A B:HEM302 4.2 28.6 1.0
C3D B:HEM302 4.2 26.5 1.0
ND1 B:MHS175 4.3 29.9 1.0
C2C B:HEM302 4.3 21.5 1.0
C3C B:HEM302 4.3 20.4 1.0
C2B B:HEM302 4.3 25.1 1.0
C3B B:HEM302 4.3 24.9 1.0
CG B:MHS175 4.3 24.8 1.0
CD1 B:TRP51 4.5 20.2 1.0
NH1 B:ARG48 4.6 16.2 0.5
CZ B:ARG48 4.8 19.2 0.5
CH2 B:TRP191 4.9 26.7 1.0
CD B:ARG48 4.9 18.8 0.5

Iron binding site 3 out of 3 in 6h08

Go back to Iron Binding Sites List in 6h08
Iron binding site 3 out of 3 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 Iron with other atoms in the Fe binding site number 3 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
C:Fe301

b:26.9
occ:1.00
FE C:HEM301 0.0 26.9 1.0
ND C:HEM301 1.9 27.5 1.0
NA C:HEM301 2.0 25.1 1.0
NC C:HEM301 2.1 26.5 1.0
NE2 C:MHS175 2.1 25.9 1.0
NB C:HEM301 2.1 28.1 1.0
O C:HOH449 2.3 52.5 1.0
C1D C:HEM301 2.9 26.3 1.0
C4D C:HEM301 2.9 26.1 1.0
C1A C:HEM301 3.0 29.0 1.0
C4B C:HEM301 3.0 29.7 1.0
C4A C:HEM301 3.0 26.9 1.0
CE1 C:MHS175 3.0 27.0 1.0
C1B C:HEM301 3.1 28.5 1.0
C4C C:HEM301 3.1 26.5 1.0
C1C C:HEM301 3.1 30.2 1.0
CD2 C:MHS175 3.1 30.5 1.0
CHA C:HEM301 3.4 27.0 1.0
CHD C:HEM301 3.4 29.8 1.0
CHC C:HEM301 3.4 27.6 1.0
CHB C:HEM301 3.4 27.4 1.0
NE1 C:TRP51 4.0 26.3 1.0
NE C:ARG48 4.0 22.1 0.5
O C:HOH455 4.1 34.9 1.0
ND1 C:MHS175 4.2 34.5 1.0
C2D C:HEM301 4.2 27.2 1.0
C3D C:HEM301 4.2 27.1 1.0
C2A C:HEM301 4.2 25.5 1.0
C3A C:HEM301 4.2 26.4 1.0
CG C:MHS175 4.3 27.8 1.0
C2C C:HEM301 4.3 25.2 1.0
C3C C:HEM301 4.3 28.3 1.0
C2B C:HEM301 4.3 30.4 1.0
C3B C:HEM301 4.3 32.5 1.0
NH2 C:ARG48 4.5 18.4 0.5
CD1 C:TRP51 4.6 26.2 1.0
CZ C:ARG48 4.8 21.9 0.5
CH2 C:TRP191 4.9 31.6 1.0
CD C:ARG48 4.9 26.1 0.5

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 Aug 6 20:23:53 2024

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