Iron in PDB 1gza: Peroxidase

All present enzymatic activity of Peroxidase:
1.11.1.7;

The structure of Peroxidase, PDB code: 1gza was solved by K.Fukuyama, H.Itakura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.06
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	74.570, 74.570, 117.470, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / n/a

The structure of Peroxidase also contains other interesting chemical elements:

Iodine	(I)	1 atom
Calcium	(Ca)	2 atoms

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

Iron binding site 1 out of 1 in the Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe345 b:14.9 occ:1.00 FE A:HEM345 0.0 14.9 1.0 ND A:HEM345 2.0 10.3 1.0 NC A:HEM345 2.0 11.4 1.0 NA A:HEM345 2.0 10.8 1.0 NB A:HEM345 2.0 13.5 1.0 NE2 A:HIS184 2.1 11.3 1.0 C1D A:HEM345 3.0 11.7 1.0 C4D A:HEM345 3.0 11.1 1.0 C4C A:HEM345 3.0 12.0 1.0 C1A A:HEM345 3.0 10.5 1.0 C1C A:HEM345 3.0 10.8 1.0 C4A A:HEM345 3.0 10.7 1.0 CD2 A:HIS184 3.0 9.6 1.0 C4B A:HEM345 3.0 13.3 1.0 C1B A:HEM345 3.0 13.5 1.0 CE1 A:HIS184 3.1 8.4 1.0 CHD A:HEM345 3.4 10.2 1.0 CHA A:HEM345 3.4 9.0 1.0 CHC A:HEM345 3.4 11.1 1.0 CHB A:HEM345 3.4 9.7 1.0 O A:HOH686 3.7 31.2 1.0 C3D A:HEM345 4.2 10.4 1.0 CG A:HIS184 4.2 8.8 1.0 C2D A:HEM345 4.2 10.4 1.0 ND1 A:HIS184 4.2 7.3 1.0 C3C A:HEM345 4.2 12.0 1.0 C2A A:HEM345 4.2 10.7 1.0 C2C A:HEM345 4.3 12.8 1.0 C3A A:HEM345 4.3 9.9 1.0 C3B A:HEM345 4.3 15.7 1.0 C2B A:HEM345 4.3 14.9 1.0

K.Fukuyama, K.Sato, H.Itakura, S.Takahashi, T.Hosoya. Binding of Iodide to Arthromyces Ramosus Peroxidase Investigated with X-Ray Crystallographic Analysis, 1H and 127I uc(Nmr) Spectroscopy, and Steady-State Kinetics. J.Biol.Chem. V. 272 5752 1997.
ISSN: ISSN 0021-9258
PubMed: 9038188
DOI: 10.1074/JBC.272.9.5752