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Iron in PDB 6y2y: The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications

Enzymatic activity of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications

All present enzymatic activity of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications:
1.11.1.5;

Protein crystallography data

The structure of The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications, PDB code: 6y2y 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) 43.22 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.97, 74.1, 106.41, 90, 90, 90
R / Rfree (%) 14.8 / 18

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications (pdb code 6y2y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications, PDB code: 6y2y:

Iron binding site 1 out of 1 in 6y2y

Go back to Iron Binding Sites List in 6y2y
Iron binding site 1 out of 1 in the The Crystal Structure of Engineered Cytochrome C Peroxidase From Saccharomyces Cerevisiae with TRP51 to S-TRP51 and TRP191PHE Modifications


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 TRP51 to S-TRP51 and TRP191PHE Modifications within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:15.0
occ:1.00
 FE A:HEM301 0.0 15.0 1.0
NB A:HEM301 2.0 14.1 1.0
NC A:HEM301 2.0 14.3 1.0
NA A:HEM301 2.0 14.9 1.0
ND A:HEM301 2.1 14.6 1.0
NE2 A:HIS175 2.1 14.3 1.0
O A:HOH559 2.3 28.1 1.0
C1C A:HEM301 3.0 14.0 1.0
C4B A:HEM301 3.0 14.7 1.0
C1A A:HEM301 3.0 15.1 1.0
C4A A:HEM301 3.1 14.4 1.0
C4D A:HEM301 3.1 14.3 1.0
C1D A:HEM301 3.1 13.1 1.0
CE1 A:HIS175 3.1 14.4 1.0
C1B A:HEM301 3.1 15.1 1.0
C4C A:HEM301 3.1 12.2 1.0
CD2 A:HIS175 3.1 14.7 1.0
CHC A:HEM301 3.4 14.2 1.0
CHA A:HEM301 3.4 15.0 1.0
CHB A:HEM301 3.4 14.6 1.0
CHD A:HEM301 3.4 12.2 1.0
ND1 A:HIS175 4.2 14.7 1.0
C2C A:HEM301 4.3 12.7 1.0
C2A A:HEM301 4.3 15.2 1.0
C2D A:HEM301 4.3 12.3 1.0
C3A A:HEM301 4.3 14.6 1.0
C3B A:HEM301 4.3 14.9 1.0
CG A:HIS175 4.3 14.0 1.0
C3D A:HEM301 4.3 13.1 1.0
C3C A:HEM301 4.3 12.0 1.0
C2B A:HEM301 4.3 15.2 1.0
S3 A:4OG51 4.4 27.3 1.0
C2 A:4OG51 4.4 23.0 1.0

Reference:

M.Ortmayer, F.J.Hardy, M.G.Quesne, K.Fisher, C.Levy, D.J.Heyes, C.R.A.Catlow, S.E.J.Rigby, S.Hay, A.P.Green. A Noncanonical Tryptophan Analogue Reveals An Active Site Hydrogen Bond Controlling Ferryl Reactivity in A Heme Peroxidase Jacs Au 2021.
ISSN: ESSN 2691-3704
DOI: 10.1021/JACSAU.1C00145
Page generated: Wed Aug 7 15:50:35 2024

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