Iron in PDB 2euu: Cytochrome C Peroxidase (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol

All present enzymatic activity of Cytochrome C Peroxidase (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol:
1.11.1.5;

The structure of Cytochrome C Peroxidase (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol, PDB code: 2euu 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)	50.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.675, 73.521, 104.674, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 16.1

The binding sites of Iron atom in the Cytochrome C Peroxidase (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol (pdb code 2euu). 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 (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol, PDB code: 2euu:

Iron binding site 1 out of 1 in the Cytochrome C Peroxidase (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol


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 (Ccp) in Complex with 1H-Imidazol-2- Ylmethanol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe295 b:11.6 occ:1.00 FE A:HEM295 0.0 11.6 1.0 NC A:HEM295 2.0 10.6 1.0 NA A:HEM295 2.0 11.4 1.0 ND A:HEM295 2.0 10.8 1.0 NB A:HEM295 2.1 10.4 1.0 NE2 A:HIS175 2.1 12.0 1.0 O A:HOH731 2.1 21.2 1.0 C1A A:HEM295 3.0 12.3 1.0 C1C A:HEM295 3.0 10.8 1.0 C1D A:HEM295 3.0 10.3 1.0 C4C A:HEM295 3.0 10.3 1.0 CD2 A:HIS175 3.1 11.1 1.0 C4D A:HEM295 3.1 10.5 1.0 C4B A:HEM295 3.1 11.5 1.0 CE1 A:HIS175 3.1 12.4 1.0 C4A A:HEM295 3.1 11.4 1.0 C1B A:HEM295 3.1 11.8 1.0 CHD A:HEM295 3.4 10.1 1.0 CHA A:HEM295 3.4 11.9 1.0 CHC A:HEM295 3.4 11.1 1.0 CHB A:HEM295 3.5 12.3 1.0 NE1 A:TRP51 4.0 14.2 1.0 NE A:ARG48 4.1 19.0 1.0 ND1 A:HIS175 4.2 12.4 1.0 CG A:HIS175 4.2 12.0 1.0 C2C A:HEM295 4.3 11.4 1.0 O A:HOH465 4.3 17.5 1.0 C2D A:HEM295 4.3 10.2 1.0 C2A A:HEM295 4.3 12.3 1.0 C3C A:HEM295 4.3 11.0 1.0 C3B A:HEM295 4.3 11.7 1.0 C3A A:HEM295 4.3 12.3 1.0 C3D A:HEM295 4.3 10.6 1.0 C2B A:HEM295 4.3 11.7 1.0 NH2 A:ARG48 4.6 17.9 1.0 CD1 A:TRP51 4.6 12.9 1.0 C2 A:BVG401 4.6 14.2 1.0 C1 A:BVG401 4.7 13.0 1.0 CZ A:ARG48 4.9 19.3 1.0 CD A:ARG48 5.0 15.9 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