Iron in PDB 2xj8: The Structure of Ferrous Cytochrome C Peroxidase

All present enzymatic activity of The Structure of Ferrous Cytochrome C Peroxidase:
1.11.1.5;

The structure of The Structure of Ferrous Cytochrome C Peroxidase, PDB code: 2xj8 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)	33.15 / 1.69
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.053, 75.193, 106.950, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21

The binding sites of Iron atom in the The Structure of Ferrous Cytochrome C Peroxidase (pdb code 2xj8). 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 Ferrous Cytochrome C Peroxidase, PDB code: 2xj8:

Iron binding site 1 out of 1 in the The Structure of Ferrous 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 Structure of Ferrous Cytochrome C Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1295 b:13.9 occ:1.00 FE A:HEM1295 0.0 13.9 1.0 O A:HOH2551 2.0 34.9 1.0 NE2 A:HIS175 2.1 15.3 1.0 NC A:HEM1295 2.1 10.8 1.0 ND A:HEM1295 2.1 11.0 1.0 NB A:HEM1295 2.1 13.7 1.0 NA A:HEM1295 2.1 11.3 1.0 C1D A:HEM1295 3.0 11.6 1.0 CE1 A:HIS175 3.0 15.9 1.0 C4B A:HEM1295 3.0 12.2 1.0 C1C A:HEM1295 3.0 12.2 1.0 C4D A:HEM1295 3.0 12.1 1.0 C4C A:HEM1295 3.1 12.1 1.0 C1A A:HEM1295 3.1 15.1 1.0 C1B A:HEM1295 3.1 12.5 1.0 CD2 A:HIS175 3.1 13.2 1.0 C4A A:HEM1295 3.1 11.7 1.0 CHC A:HEM1295 3.4 8.2 1.0 CHD A:HEM1295 3.4 11.2 1.0 CHA A:HEM1295 3.4 11.7 1.0 CHB A:HEM1295 3.5 11.4 1.0 NE A:ARG48 4.1 7.2 0.5 NE1 A:TRP51 4.1 13.4 1.0 ND1 A:HIS175 4.1 13.0 1.0 CG A:HIS175 4.2 13.0 1.0 C2D A:HEM1295 4.2 12.3 1.0 O A:HOH2169 4.2 22.1 1.0 C3B A:HEM1295 4.3 13.2 1.0 C3D A:HEM1295 4.3 13.9 1.0 C2B A:HEM1295 4.3 12.9 1.0 C3C A:HEM1295 4.3 12.1 1.0 C2C A:HEM1295 4.3 12.8 1.0 C2A A:HEM1295 4.3 13.7 1.0 C3A A:HEM1295 4.3 12.8 1.0 CD1 A:TRP51 4.7 11.8 1.0 NH2 A:ARG48 4.7 14.9 0.5 CZ A:ARG48 4.9 9.0 0.5

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