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Iron in PDB 1cmu: The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase

Enzymatic activity of The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase

All present enzymatic activity of The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase, PDB code: 1cmu was solved by M.M.Fitzgerald, M.L.Trester, 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) 5.00 / 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 (%) 19.6 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase (pdb code 1cmu). 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 Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase, PDB code: 1cmu:

Iron binding site 1 out of 1 in 1cmu

Go back to Iron Binding Sites List in 1cmu
Iron binding site 1 out of 1 in the The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:16.8
occ:1.00
 FE A:HEM295 0.0 16.8 1.0
O A:HOH313 1.9 12.4 1.0
NC A:HEM295 2.0 13.3 1.0
NE2 A:HIS175 2.0 20.8 1.0
NA A:HEM295 2.1 14.3 1.0
ND A:HEM295 2.1 14.5 1.0
NB A:HEM295 2.1 12.8 1.0
CE1 A:HIS175 2.7 24.7 1.0
C4C A:HEM295 3.0 10.5 1.0
C1D A:HEM295 3.0 10.1 1.0
C1A A:HEM295 3.1 14.9 1.0
C1C A:HEM295 3.1 12.4 1.0
C4A A:HEM295 3.1 13.1 1.0
C4D A:HEM295 3.1 8.3 1.0
C4B A:HEM295 3.1 11.1 1.0
C1B A:HEM295 3.1 12.7 1.0
CD2 A:HIS175 3.2 24.2 1.0
CHD A:HEM295 3.3 9.8 1.0
CHC A:HEM295 3.4 11.8 1.0
CHA A:HEM295 3.4 7.8 1.0
CHB A:HEM295 3.4 10.7 1.0
ND1 A:HIS175 3.9 25.9 1.0
NE1 A:TRP51 4.1 20.6 1.0
CG A:HIS175 4.2 21.3 1.0
C3C A:HEM295 4.2 10.0 1.0
C2D A:HEM295 4.2 11.5 1.0
C2C A:HEM295 4.2 11.0 1.0
C2A A:HEM295 4.2 14.3 1.0
C3A A:HEM295 4.2 13.8 1.0
C3D A:HEM295 4.2 11.6 1.0
C3B A:HEM295 4.3 10.4 1.0
O A:HOH300 4.3 46.0 1.0
C2B A:HEM295 4.3 9.5 1.0
CD1 A:TRP51 4.5 16.8 1.0
O A:HOH344 4.5 32.9 1.0

Reference:

M.M.Fitzgerald, M.L.Trester, G.M.Jensen, D.E.Mcree, D.B.Goodin. The Role of Aspartate-235 in the Binding of Cations to An Artificial Cavity at the Radical Site of Cytochrome C Peroxidase. Protein Sci. V. 4 1844 1995.
ISSN: ISSN 0961-8368
PubMed: 8528082
Page generated: Sat Aug 3 03:24:02 2024

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