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Iron in PDB 1ebe: Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I

Enzymatic activity of Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I

All present enzymatic activity of Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I:
1.11.1.5;

Protein crystallography data

The structure of Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I, PDB code: 1ebe was solved by V.Fulop, R.P.Phizackerley, S.M.Soltis, I.J.Clifton, S.Wakatsuki, J.E.Erman, J.Hajdu, S.L.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 107.400, 76.800, 51.400, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I (pdb code 1ebe). 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 Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I, PDB code: 1ebe:

Iron binding site 1 out of 1 in 1ebe

Go back to Iron Binding Sites List in 1ebe
Iron binding site 1 out of 1 in the Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1295

b:29.7
occ:1.00
FE A:HEM1295 0.0 29.7 1.0
O A:O1296 1.7 30.2 1.0
NC A:HEM1295 1.9 24.2 1.0
NA A:HEM1295 2.0 28.8 1.0
NB A:HEM1295 2.0 24.6 1.0
ND A:HEM1295 2.0 30.9 1.0
NE2 A:HIS175 2.0 25.7 1.0
CD2 A:HIS175 2.9 27.7 1.0
C4C A:HEM1295 3.0 28.4 1.0
C4A A:HEM1295 3.0 30.5 1.0
C1B A:HEM1295 3.0 27.5 1.0
C1C A:HEM1295 3.0 25.3 1.0
C1D A:HEM1295 3.0 26.6 1.0
C1A A:HEM1295 3.0 29.6 1.0
CE1 A:HIS175 3.1 26.1 1.0
C4B A:HEM1295 3.1 24.0 1.0
C4D A:HEM1295 3.1 26.2 1.0
CHD A:HEM1295 3.3 31.7 1.0
CHB A:HEM1295 3.4 31.7 1.0
CHA A:HEM1295 3.5 28.1 1.0
CHC A:HEM1295 3.5 24.7 1.0
O A:HOH2057 3.8 32.6 1.0
NE1 A:TRP51 3.9 23.4 1.0
NE A:ARG48 4.1 28.6 1.0
CG A:HIS175 4.1 26.4 1.0
ND1 A:HIS175 4.2 24.2 1.0
C3C A:HEM1295 4.2 28.1 1.0
C2C A:HEM1295 4.2 28.4 1.0
C2A A:HEM1295 4.3 27.7 1.0
C3A A:HEM1295 4.3 25.7 1.0
C2D A:HEM1295 4.3 22.3 1.0
C2B A:HEM1295 4.3 24.1 1.0
C3D A:HEM1295 4.3 24.6 1.0
C3B A:HEM1295 4.3 23.4 1.0
CD1 A:TRP51 4.5 28.9 1.0
NH1 A:ARG48 4.6 27.5 1.0
CE2 A:TRP51 4.8 27.4 1.0
CG A:ARG48 4.8 27.9 1.0
CZ A:ARG48 4.8 27.1 1.0
CD A:ARG48 5.0 27.7 1.0

Reference:

V.Fulop, R.P.Phizackerley, S.M.Soltis, I.J.Clifton, S.Wakatsuki, J.E.Erman, J.Hajdu, S.L.Edwards. Laue Diffraction Study on the Structure of Cytochrome C Peroxidase Compound I Structure V. 2 201 1994.
ISSN: ISSN 0969-2126
PubMed: 8069633
DOI: 10.1016/S0969-2126(00)00021-6
Page generated: Sun Dec 13 14:12:22 2020

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