Iron in PDB 2as4: Cytochrome C Peroxidase in Complex with 3-Fluorocatechol

All present enzymatic activity of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol:
1.11.1.5;

The structure of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4 was solved by R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.240, 75.490, 107.040, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / 17.5

The structure of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol also contains other interesting chemical elements:

Fluorine	(F)	2 atoms
Potassium	(K)	1 atom

The binding sites of Iron atom in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol (pdb code 2as4). 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 Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4:

Iron binding site 1 out of 1 in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:13.7 occ:1.00 FE A:HEM400 0.0 13.7 1.0 NC A:HEM400 2.0 13.2 1.0 NA A:HEM400 2.1 14.8 1.0 ND A:HEM400 2.1 14.6 1.0 NE2 A:HIS175 2.1 14.3 1.0 NB A:HEM400 2.1 15.3 1.0 O A:HOH1415 2.1 26.2 1.0 CE1 A:HIS175 3.0 15.5 1.0 C1C A:HEM400 3.0 13.9 1.0 C1A A:HEM400 3.0 15.0 1.0 C4B A:HEM400 3.0 13.7 1.0 C4D A:HEM400 3.1 14.8 1.0 C4C A:HEM400 3.1 13.5 1.0 C4A A:HEM400 3.1 14.9 1.0 C1D A:HEM400 3.1 13.9 1.0 C1B A:HEM400 3.1 13.8 1.0 CD2 A:HIS175 3.1 15.5 1.0 CHC A:HEM400 3.3 13.8 1.0 CHA A:HEM400 3.4 15.4 1.0 CHD A:HEM400 3.4 13.5 1.0 CHB A:HEM400 3.4 14.8 1.0 NE A:ARG48 4.0 16.9 0.6 NE1 A:TRP51 4.0 17.1 1.0 ND1 A:HIS175 4.2 14.7 1.0 C2A A:HEM400 4.2 15.2 1.0 CG A:HIS175 4.2 14.2 1.0 C2C A:HEM400 4.2 14.0 1.0 O A:HOH1200 4.2 23.7 1.0 C3C A:HEM400 4.2 13.2 1.0 C3A A:HEM400 4.3 15.5 1.0 C3B A:HEM400 4.3 13.4 1.0 C3D A:HEM400 4.3 14.0 1.0 C2D A:HEM400 4.3 13.6 1.0 C2B A:HEM400 4.3 14.3 1.0 O A:HOH1003 4.5 25.7 0.2 CD1 A:TRP51 4.6 16.2 1.0 NH2 A:ARG48 4.6 15.3 0.6 CD A:ARG48 4.8 15.6 0.6 CZ A:ARG48 4.8 16.6 0.6 CG A:ARG48 4.9 15.9 0.6 C6 A:3FA500 4.9 26.0 0.8

R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet. Probing Molecular Docking in A Charged Model Binding Site. J.Mol.Biol. V. 357 1449 2006.
ISSN: ISSN 0022-2836
PubMed: 16490206
DOI: 10.1016/J.JMB.2006.01.034