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Iron in PDB 2x08: Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site

Enzymatic activity of Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site

All present enzymatic activity of Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site:
1.11.1.5;

Protein crystallography data

The structure of Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site, PDB code: 2x08 was solved by E.J.Murphy, C.L.Metcalfe, A.Gumiero, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.92 / 2.01
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.000, 74.490, 106.470, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site (pdb code 2x08). 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 Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site, PDB code: 2x08:

Iron binding site 1 out of 1 in 2x08

Go back to Iron Binding Sites List in 2x08
Iron binding site 1 out of 1 in the Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase: Ascorbate Bound to the Engineered Ascorbate Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1254

b:24.8
occ:1.00
FE A:HEM1254 0.0 24.8 1.0
NB A:HEM1254 2.0 24.6 1.0
NC A:HEM1254 2.1 23.4 1.0
ND A:HEM1254 2.1 24.8 1.0
NE2 A:HIS175 2.1 21.1 1.0
NA A:HEM1254 2.1 23.8 1.0
O A:HOH2042 2.3 38.0 1.0
CE1 A:HIS175 3.0 21.0 1.0
C4C A:HEM1254 3.0 21.1 1.0
C4B A:HEM1254 3.0 22.5 1.0
C1C A:HEM1254 3.0 22.1 1.0
C4D A:HEM1254 3.1 22.9 1.0
C1D A:HEM1254 3.1 21.9 1.0
C1B A:HEM1254 3.1 24.5 1.0
C1A A:HEM1254 3.1 23.8 1.0
CD2 A:HIS175 3.1 17.1 1.0
C4A A:HEM1254 3.2 25.3 1.0
CHC A:HEM1254 3.4 19.9 1.0
CHD A:HEM1254 3.4 19.8 1.0
CHA A:HEM1254 3.4 22.1 1.0
CHB A:HEM1254 3.5 23.6 1.0
NE1 A:TRP51 4.0 20.1 1.0
NE A:ARG48 4.1 25.8 1.0
ND1 A:HIS175 4.1 19.9 1.0
CG A:HIS175 4.2 20.0 1.0
C3C A:HEM1254 4.3 20.0 1.0
C2C A:HEM1254 4.3 18.0 1.0
C3D A:HEM1254 4.3 23.1 1.0
C2D A:HEM1254 4.3 22.8 1.0
C3B A:HEM1254 4.3 23.5 1.0
C2B A:HEM1254 4.3 22.4 1.0
O A:HOH2046 4.3 24.6 1.0
C2A A:HEM1254 4.4 22.7 1.0
C3A A:HEM1254 4.4 22.3 1.0
CD1 A:TRP51 4.5 23.2 1.0
NH2 A:ARG48 4.6 20.9 1.0
CZ A:ARG48 4.8 26.6 1.0
CD A:ARG48 4.9 25.1 1.0

Reference:

E.J.Murphy, C.L.Metcalfe, J.Basran, P.C.Moody, E.L.Raven. Engineering the Substrate Specificity and Reactivity of A Heme Protein: Creation of An Ascorbate Binding Site in Cytochrome C Peroxidase. Biochemistry V. 47 13933 2008.
ISSN: ISSN 1520-4995
PubMed: 19061385
DOI: 10.1021/BI801480R
Page generated: Sun Dec 13 14:56:10 2020

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