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Iron in PDB 3e2o: Crystal Structure of Cytochrome C Peroxidase, N184R Mutant

Enzymatic activity of Crystal Structure of Cytochrome C Peroxidase, N184R Mutant

All present enzymatic activity of Crystal Structure of Cytochrome C Peroxidase, N184R Mutant:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of Cytochrome C Peroxidase, N184R Mutant, PDB code: 3e2o was solved by T.L.Poulos, Y.T.Meharenna, P.Oertel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.06
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 107.304, 75.916, 51.223, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 19.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Cytochrome C Peroxidase, N184R Mutant (pdb code 3e2o). 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 Crystal Structure of Cytochrome C Peroxidase, N184R Mutant, PDB code: 3e2o:

Iron binding site 1 out of 1 in 3e2o

Go back to Iron Binding Sites List in 3e2o
Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome C Peroxidase, N184R Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Cytochrome C Peroxidase, N184R Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:9.2
occ:1.00
FE A:HEM296 0.0 9.2 1.0
O A:HOH1541 2.0 22.0 1.0
NC A:HEM296 2.0 9.6 1.0
ND A:HEM296 2.0 9.7 1.0
NA A:HEM296 2.0 10.9 1.0
NB A:HEM296 2.0 9.8 1.0
NE2 A:HIS175 2.1 10.7 1.0
C4D A:HEM296 3.0 9.4 1.0
C4C A:HEM296 3.0 8.3 1.0
C1C A:HEM296 3.0 9.3 1.0
C1A A:HEM296 3.0 10.4 1.0
C4B A:HEM296 3.0 9.7 1.0
C4A A:HEM296 3.1 9.4 1.0
C1D A:HEM296 3.1 8.8 1.0
CE1 A:HIS175 3.1 10.5 1.0
C1B A:HEM296 3.1 10.2 1.0
CD2 A:HIS175 3.1 10.5 1.0
CHC A:HEM296 3.4 9.7 1.0
CHA A:HEM296 3.4 10.8 1.0
CHD A:HEM296 3.4 9.1 1.0
CHB A:HEM296 3.5 10.8 1.0
NE1 A:TRP51 4.0 11.8 1.0
NE A:ARG48 4.2 13.5 1.0
ND1 A:HIS175 4.2 10.3 1.0
O A:HOH1115 4.2 18.1 1.0
C3D A:HEM296 4.3 10.0 1.0
C2C A:HEM296 4.3 9.8 1.0
C2D A:HEM296 4.3 8.8 1.0
CG A:HIS175 4.3 9.2 1.0
C3A A:HEM296 4.3 10.5 1.0
C2A A:HEM296 4.3 10.0 1.0
C3C A:HEM296 4.3 9.5 1.0
C2B A:HEM296 4.3 9.3 1.0
C3B A:HEM296 4.3 10.2 1.0
NH2 A:ARG48 4.6 13.8 1.0
CD1 A:TRP51 4.7 11.6 1.0
CZ A:ARG48 4.9 13.0 1.0

Reference:

Y.T.Meharenna, P.Oertel, B.Bhaskar, T.L.Poulos. Engineering Ascorbate Peroxidase Activity Into Cytochrome C Peroxidase. Biochemistry V. 47 10324 2008.
ISSN: ISSN 0006-2960
PubMed: 18771292
DOI: 10.1021/BI8007565
Page generated: Sun Aug 4 09:18:48 2024

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