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Iron in PDB 1aev: Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole)

Enzymatic activity of Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole)

All present enzymatic activity of Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole):
1.11.1.5;

Protein crystallography data

The structure of Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole), PDB code: 1aev was solved by R.A.Musah, M.M.Fitzgerald, G.M.Jensen, D.E.Mcree, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.200, 74.300, 45.400, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole) (pdb code 1aev). 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 Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole), PDB code: 1aev:

Iron binding site 1 out of 1 in 1aev

Go back to Iron Binding Sites List in 1aev
Iron binding site 1 out of 1 in the Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2- Aminothiazole and Covalent Modification of the Enzyme (2- Aminothiazole) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:16.0
occ:1.00
 FE A:HEM295 0.0 16.0 1.0
O A:HOH313 2.0 22.2 1.0
NE2 A:HIS175 2.0 17.3 1.0
NC A:HEM295 2.0 13.4 1.0
NA A:HEM295 2.1 12.7 1.0
ND A:HEM295 2.1 15.7 1.0
NB A:HEM295 2.1 16.4 1.0
CE1 A:HIS175 2.8 10.9 1.0
C4C A:HEM295 3.0 15.8 1.0
C1C A:HEM295 3.0 15.5 1.0
C1A A:HEM295 3.0 13.7 1.0
C4D A:HEM295 3.1 12.7 1.0
C1D A:HEM295 3.1 9.5 1.0
C4B A:HEM295 3.1 11.4 1.0
CD2 A:HIS175 3.1 17.1 1.0
C4A A:HEM295 3.1 13.2 1.0
C1B A:HEM295 3.1 13.4 1.0
CHC A:HEM295 3.4 11.2 1.0
CHD A:HEM295 3.4 13.1 1.0
CHA A:HEM295 3.4 11.3 1.0
CHB A:HEM295 3.4 14.0 1.0
HE1 A:TRP51 3.6 0.0 1.0
ND1 A:HIS175 4.0 12.1 1.0
CG A:HIS175 4.2 14.7 1.0
NE1 A:TRP51 4.2 21.0 1.0
C3C A:HEM295 4.2 14.8 1.0
C3D A:HEM295 4.2 14.5 1.0
C2D A:HEM295 4.2 11.3 1.0
C2A A:HEM295 4.2 12.2 1.0
C2C A:HEM295 4.2 12.1 1.0
C3A A:HEM295 4.3 10.9 1.0
C3B A:HEM295 4.3 12.3 1.0
C2B A:HEM295 4.3 14.3 1.0
O A:HOH344 4.4 37.8 1.0
C5 A:AMT296 4.4 22.7 1.0
O A:HOH300 4.5 30.0 1.0
CD1 A:TRP51 4.6 19.9 1.0
HD1 A:HIS175 4.8 0.0 1.0
HE A:ARG48 4.8 0.0 1.0
S1 A:AMT296 4.9 25.5 1.0

Reference:

R.A.Musah, D.B.Goodin. Introduction of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation of 2-Aminothiazole and Covalent Modification of the Enzyme. Biochemistry V. 36 11665 1997.
ISSN: ISSN 0006-2960
PubMed: 9305956
DOI: 10.1021/BI9708038
Page generated: Wed Jul 16 12:08:23 2025

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