Iron in PDB 1gzb: Peroxidase

All present enzymatic activity of Peroxidase:
1.11.1.7;

The structure of Peroxidase, PDB code: 1gzb was solved by K.Fukuyama, N.Kunishima, F.Amada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.80
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 (%)	18.8 / n/a

The structure of Peroxidase also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

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

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:13.1 occ:1.00 FE A:HEM345 0.0 13.1 1.0 NA A:HEM345 2.0 11.0 1.0 ND A:HEM345 2.0 10.4 1.0 NB A:HEM345 2.0 11.6 1.0 NC A:HEM345 2.0 11.8 1.0 NE2 A:HIS184 2.1 11.9 1.0 C1D A:HEM345 3.0 11.2 1.0 C4A A:HEM345 3.0 10.7 1.0 C4D A:HEM345 3.0 10.2 1.0 C1A A:HEM345 3.0 10.8 1.0 C4C A:HEM345 3.0 12.2 1.0 C1B A:HEM345 3.0 11.3 1.0 C4B A:HEM345 3.0 12.4 1.0 C1C A:HEM345 3.0 12.1 1.0 CD2 A:HIS184 3.1 10.1 1.0 CE1 A:HIS184 3.1 10.7 1.0 CHD A:HEM345 3.4 11.4 1.0 CHB A:HEM345 3.4 10.3 1.0 CHC A:HEM345 3.4 11.8 1.0 CHA A:HEM345 3.4 10.6 1.0 O A:HOH686 3.9 18.5 1.0 C2D A:HEM345 4.2 11.1 1.0 C3D A:HEM345 4.2 10.8 1.0 C2A A:HEM345 4.2 10.4 1.0 C3A A:HEM345 4.2 11.1 1.0 CG A:HIS184 4.2 11.3 1.0 ND1 A:HIS184 4.3 11.9 1.0 C2C A:HEM345 4.3 11.9 1.0 C2B A:HEM345 4.3 12.7 1.0 C3C A:HEM345 4.3 13.2 1.0 C3B A:HEM345 4.3 14.4 1.0

N.Kunishima, F.Amada, K.Fukuyama, M.Kawamoto, T.Matsunaga, H.Matsubara. Pentacoordination of the Heme Iron of Arthromyces Ramosus Peroxidase Shown By A 1.8 A Resolution Crystallographic Study at pH 4.5. Febs Lett. V. 378 291 1996.
ISSN: ISSN 0014-5793
PubMed: 8557120
DOI: 10.1016/0014-5793(95)01458-6