Iron in PDB 2cpo: Chloroperoxidase

All present enzymatic activity of Chloroperoxidase:
1.11.1.10;

The structure of Chloroperoxidase, PDB code: 2cpo was solved by M.Sundaramoorthy, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	58.620, 152.170, 102.100, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 22.8

The structure of Chloroperoxidase also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Iron atom in the Chloroperoxidase (pdb code 2cpo). 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 Chloroperoxidase, PDB code: 2cpo:

Iron binding site 1 out of 1 in the Chloroperoxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Chloroperoxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe396 b:14.2 occ:1.00 FE A:HEM396 0.0 14.2 1.0 NA A:HEM396 2.0 12.7 1.0 ND A:HEM396 2.0 15.6 1.0 NC A:HEM396 2.0 14.8 1.0 NB A:HEM396 2.1 13.2 1.0 SG A:CYS29 2.3 10.1 1.0 O A:HOH801 3.0 31.5 1.0 C1A A:HEM396 3.0 14.1 1.0 C4D A:HEM396 3.0 12.3 1.0 C4A A:HEM396 3.1 14.2 1.0 C1C A:HEM396 3.1 13.6 1.0 C1D A:HEM396 3.1 12.3 1.0 C4C A:HEM396 3.1 13.3 1.0 C4B A:HEM396 3.1 12.8 1.0 C1B A:HEM396 3.1 9.4 1.0 CHA A:HEM396 3.4 14.5 1.0 CHC A:HEM396 3.5 12.0 1.0 CB A:CYS29 3.5 10.2 1.0 CHD A:HEM396 3.5 11.9 1.0 CHB A:HEM396 3.5 9.6 1.0 C2A A:HEM396 4.2 13.0 1.0 C3A A:HEM396 4.3 8.5 1.0 C3D A:HEM396 4.3 11.1 1.0 C2D A:HEM396 4.3 12.7 1.0 C2C A:HEM396 4.3 11.9 1.0 C3C A:HEM396 4.3 13.5 1.0 C3B A:HEM396 4.3 14.4 1.0 C2B A:HEM396 4.4 12.2 1.0 CA A:CYS29 4.4 10.8 1.0 CE2 A:PHE186 4.6 9.5 1.0 CD2 A:PHE186 4.7 9.0 1.0 CB A:ALA31 4.9 6.2 1.0 OE2 A:GLU183 4.9 15.0 1.0

M.Sundaramoorthy, J.Terner, T.L.Poulos. The Crystal Structure of Chloroperoxidase: A Heme Peroxidase--Cytochrome P450 Functional Hybrid. Structure V. 3 1367 1995.
ISSN: ISSN 0969-2126
PubMed: 8747463
DOI: 10.1016/S0969-2126(01)00274-X