Iron in PDB 2as1: Cytochrome C Peroxidase in Complex with Thiopheneamidine

All present enzymatic activity of Cytochrome C Peroxidase in Complex with Thiopheneamidine:
1.11.1.5;

The structure of Cytochrome C Peroxidase in Complex with Thiopheneamidine, PDB code: 2as1 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 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.076, 76.023, 107.164, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 20

The binding sites of Iron atom in the Cytochrome C Peroxidase in Complex with Thiopheneamidine (pdb code 2as1). 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 Thiopheneamidine, PDB code: 2as1:

Iron binding site 1 out of 1 in the Cytochrome C Peroxidase in Complex with Thiopheneamidine


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 Thiopheneamidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:10.8 occ:1.00 FE A:HEM400 0.0 10.8 1.0 NA A:HEM400 2.0 10.9 1.0 NC A:HEM400 2.0 9.5 1.0 NE2 A:HIS175 2.1 11.1 1.0 ND A:HEM400 2.1 10.8 1.0 NB A:HEM400 2.1 11.0 1.0 O A:HOH1415 2.2 13.6 1.0 CE1 A:HIS175 3.0 10.6 1.0 C1A A:HEM400 3.0 11.9 1.0 C1C A:HEM400 3.0 10.5 1.0 C4A A:HEM400 3.0 10.9 1.0 C1D A:HEM400 3.1 11.0 1.0 C4B A:HEM400 3.1 9.9 1.0 C4C A:HEM400 3.1 9.4 1.0 C4D A:HEM400 3.1 11.6 1.0 C1B A:HEM400 3.1 9.9 1.0 CD2 A:HIS175 3.1 10.7 1.0 CHC A:HEM400 3.4 9.8 1.0 CHA A:HEM400 3.4 12.8 1.0 CHB A:HEM400 3.4 10.1 1.0 CHD A:HEM400 3.4 9.7 1.0 NE1 A:TRP51 4.0 13.1 1.0 ND1 A:HIS175 4.1 10.0 1.0 C2A A:HEM400 4.2 12.2 1.0 C3A A:HEM400 4.2 11.8 1.0 CG A:HIS175 4.2 11.4 1.0 C2C A:HEM400 4.2 10.1 1.0 C3C A:HEM400 4.3 10.2 1.0 O A:HOH1200 4.3 17.9 1.0 C2D A:HEM400 4.3 11.1 1.0 C2B A:HEM400 4.3 10.6 1.0 C3D A:HEM400 4.3 10.8 1.0 C3B A:HEM400 4.3 10.5 1.0 C5 A:TP5500 4.4 11.4 1.0 CD1 A:TRP51 4.5 12.6 1.0 O A:HOH1505 4.6 23.2 1.0

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