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Iron in PDB 1cck: Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202

Enzymatic activity of Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202

All present enzymatic activity of Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202:
1.11.1.5;

Protein crystallography data

The structure of Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202, PDB code: 1cck was solved by Y.Cao, R.A.Musah, S.K.Wilcox, D.B.Goodin, D.E.Mcree, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 103.500, 73.400, 44.700, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202 (pdb code 1cck). 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 Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202, PDB code: 1cck:

Iron binding site 1 out of 1 in 1cck

Go back to Iron Binding Sites List in 1cck
Iron binding site 1 out of 1 in the Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Altering Substrate Specificity of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosine For Phe 202 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:17.0
occ:1.00
 FE A:HEM1 0.0 17.0 1.0
NA A:HEM1 2.0 12.8 1.0
NE2 A:HIS175 2.0 19.0 1.0
NC A:HEM1 2.1 14.0 1.0
ND A:HEM1 2.1 15.8 1.0
NB A:HEM1 2.1 14.8 1.0
O A:HOH313 2.2 25.5 1.0
CE1 A:HIS175 2.9 15.9 1.0
C1A A:HEM1 3.0 14.9 1.0
C4A A:HEM1 3.0 15.7 1.0
C4D A:HEM1 3.0 9.6 1.0
C4C A:HEM1 3.0 15.9 1.0
CD2 A:HIS175 3.1 18.0 1.0
C1B A:HEM1 3.1 12.4 1.0
C1D A:HEM1 3.1 9.4 1.0
C4B A:HEM1 3.1 11.2 1.0
C1C A:HEM1 3.1 15.4 1.0
CHA A:HEM1 3.3 13.3 1.0
CHD A:HEM1 3.4 10.3 1.0
CHB A:HEM1 3.4 13.7 1.0
CHC A:HEM1 3.4 13.2 1.0
HE1 A:TRP51 3.8 0.0 1.0
ND1 A:HIS175 4.1 13.4 1.0
CG A:HIS175 4.2 17.2 1.0
C2A A:HEM1 4.2 13.3 1.0
C3A A:HEM1 4.2 10.2 1.0
C3D A:HEM1 4.2 13.4 1.0
C2D A:HEM1 4.2 12.4 1.0
C3C A:HEM1 4.3 15.1 1.0
C3B A:HEM1 4.3 15.9 1.0
C2B A:HEM1 4.3 18.1 1.0
C2C A:HEM1 4.3 14.9 1.0
NE1 A:TRP51 4.3 22.5 1.0
O A:HOH300 4.7 41.4 1.0
CD1 A:TRP51 4.7 17.8 1.0
O A:HOH344 4.7 50.5 1.0
HE A:ARG48 4.8 0.0 1.0
HD1 A:HIS175 4.9 0.0 1.0
CH2 A:TRP191 5.0 13.8 1.0

Reference:

W.R.Patterson, T.L.Poulos. Crystal Structure of Recombinant Pea Cytosolic Ascorbate Peroxidase. Biochemistry V. 34 4331 1995.
ISSN: ISSN 0006-2960
PubMed: 7703247
DOI: 10.1021/BI00013A023
Page generated: Sun Dec 13 14:08:48 2020

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