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Iron in PDB 2xi6: The Structure of Ascorbate Peroxidase Compound I

Enzymatic activity of The Structure of Ascorbate Peroxidase Compound I

All present enzymatic activity of The Structure of Ascorbate Peroxidase Compound I:
1.11.1.11;

Protein crystallography data

The structure of The Structure of Ascorbate Peroxidase Compound I, PDB code: 2xi6 was solved by 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) 10.00 / 1.65
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.030, 82.030, 75.190, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17.6

Other elements in 2xi6:

The structure of The Structure of Ascorbate Peroxidase Compound I also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the The Structure of Ascorbate Peroxidase Compound I (pdb code 2xi6). 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 Structure of Ascorbate Peroxidase Compound I, PDB code: 2xi6:

Iron binding site 1 out of 1 in 2xi6

Go back to Iron Binding Sites List in 2xi6
Iron binding site 1 out of 1 in the The Structure of Ascorbate 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 The Structure of Ascorbate Peroxidase Compound I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe288

b:12.7
occ:1.00
FE A:HEM288 0.0 12.7 1.0
O A:HOH2456 1.7 17.6 1.0
NE2 A:HIS163 2.0 14.2 1.0
ND A:HEM288 2.1 10.1 1.0
NC A:HEM288 2.1 12.6 1.0
NA A:HEM288 2.1 14.7 1.0
NB A:HEM288 2.1 13.1 1.0
C1D A:HEM288 3.0 12.5 1.0
C1C A:HEM288 3.0 16.1 1.0
CD2 A:HIS163 3.0 13.3 1.0
C4D A:HEM288 3.0 13.1 1.0
C1A A:HEM288 3.0 15.0 1.0
C4C A:HEM288 3.0 14.9 1.0
C4B A:HEM288 3.1 11.2 1.0
CE1 A:HIS163 3.1 13.1 1.0
C1B A:HEM288 3.1 14.7 1.0
C4A A:HEM288 3.1 13.7 1.0
CHA A:HEM288 3.4 15.6 1.0
CHC A:HEM288 3.4 9.8 1.0
CHD A:HEM288 3.4 12.0 1.0
CHB A:HEM288 3.5 11.1 1.0
O A:HOH2106 3.9 19.7 0.5
NE1 A:TRP41 4.0 16.9 1.0
NE A:ARG38 4.1 28.6 0.5
C2D A:HEM288 4.2 11.4 1.0
CG A:HIS163 4.2 15.2 1.0
ND1 A:HIS163 4.2 14.8 1.0
O A:HOH2116 4.2 26.7 1.0
C3D A:HEM288 4.2 9.9 1.0
C2C A:HEM288 4.2 11.1 1.0
C3C A:HEM288 4.3 10.1 1.0
C2A A:HEM288 4.3 13.4 1.0
C3B A:HEM288 4.3 12.6 1.0
C3A A:HEM288 4.3 13.2 1.0
C2B A:HEM288 4.3 16.0 1.0
CD1 A:TRP41 4.5 12.2 1.0
NH2 A:ARG38 4.8 10.0 0.5
CD A:ARG38 4.9 17.3 0.5
CZ A:ARG38 4.9 26.9 0.5

Reference:

A.Gumiero, C.L.Metcalfe, A.R.Pearson, E.L.Raven, P.C.Moody. Nature of the Ferryl Heme in Compounds I and II. J. Biol. Chem. V. 286 1260 2011.
ISSN: ESSN 1083-351X
PubMed: 21062738
DOI: 10.1074/JBC.M110.183483
Page generated: Sun Dec 13 14:56:25 2020

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