Iron in PDB 1mnp: Manganese Peroxidase

All present enzymatic activity of Manganese Peroxidase:
1.11.1.7;

The structure of Manganese Peroxidase, PDB code: 1mnp 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 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	163.240, 45.970, 53.715, 90.00, 97.16, 90.00
R / Rfree (%)	20 / n/a

The structure of Manganese Peroxidase also contains other interesting chemical elements:

Manganese	(Mn)	1 atom
Calcium	(Ca)	2 atoms

The binding sites of Iron atom in the Manganese Peroxidase (pdb code 1mnp). 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 Manganese Peroxidase, PDB code: 1mnp:

Iron binding site 1 out of 1 in the Manganese Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Manganese Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe396 b:7.6 occ:1.00 FE A:HEM396 0.0 7.6 1.0 ND A:HEM396 2.0 4.1 1.0 NA A:HEM396 2.0 3.6 1.0 NC A:HEM396 2.0 4.4 1.0 NB A:HEM396 2.0 4.0 1.0 NE2 A:HIS173 2.3 5.6 1.0 O A:HOH556 2.8 6.7 1.0 C4D A:HEM396 3.0 4.3 1.0 C1D A:HEM396 3.0 5.4 1.0 C1A A:HEM396 3.0 3.9 1.0 C4C A:HEM396 3.0 5.4 1.0 C4A A:HEM396 3.1 6.2 1.0 C1C A:HEM396 3.1 4.6 1.0 C4B A:HEM396 3.1 5.7 1.0 C1B A:HEM396 3.1 3.8 1.0 CD2 A:HIS173 3.2 4.8 1.0 CE1 A:HIS173 3.3 6.1 1.0 CHA A:HEM396 3.4 4.9 1.0 CHD A:HEM396 3.4 7.6 1.0 CHC A:HEM396 3.4 5.6 1.0 CHB A:HEM396 3.5 2.6 1.0 C3D A:HEM396 4.2 4.8 1.0 C2D A:HEM396 4.2 3.5 1.0 C2A A:HEM396 4.3 3.4 1.0 C3A A:HEM396 4.3 4.3 1.0 C3C A:HEM396 4.3 4.9 1.0 C2C A:HEM396 4.3 6.7 1.0 C3B A:HEM396 4.3 7.3 1.0 C2B A:HEM396 4.3 5.4 1.0 CG A:HIS173 4.4 7.1 1.0 ND1 A:HIS173 4.4 6.3 1.0

M.Sundaramoorthy, K.Kishi, M.H.Gold, T.L.Poulos. Preliminary Crystallographic Analysis of Manganese Peroxidase From Phanerochaete Chrysosporium. J.Mol.Biol. V. 238 845 1994.
ISSN: ISSN 0022-2836
PubMed: 8182752
DOI: 10.1006/JMBI.1994.1338