Iron in PDB 4cjo: Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced at 180K Using X-Rays

The structure of Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced at 180K Using X-Rays, PDB code: 4cjo was solved by D.Kekilli, F.Dworkowski, S.Antonyuk, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.48 / 1.55
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.675, 53.675, 181.812, 90.00, 90.00, 120.00
R / Rfree (%)	23.12 / 25.119

The binding sites of Iron atom in the Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced at 180K Using X-Rays (pdb code 4cjo). 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 Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced at 180K Using X-Rays, PDB code: 4cjo:

Iron binding site 1 out of 1 in the Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced at 180K Using X-Rays


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced at 180K Using X-Rays within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:14.5 occ:1.00 FE A:HEC128 0.0 14.5 1.0 NC A:HEC128 2.0 15.1 1.0 NA A:HEC128 2.0 14.3 1.0 NE2 A:HIS120 2.0 15.0 1.0 ND A:HEC128 2.0 14.0 1.0 NB A:HEC128 2.1 15.3 1.0 CD2 A:HIS120 3.0 16.1 1.0 C1D A:HEC128 3.0 13.6 1.0 C4C A:HEC128 3.0 14.2 1.0 C1C A:HEC128 3.0 14.6 1.0 CE1 A:HIS120 3.1 17.3 1.0 C1A A:HEC128 3.1 14.4 1.0 C4A A:HEC128 3.1 14.4 1.0 C4D A:HEC128 3.1 14.0 1.0 C4B A:HEC128 3.1 15.4 1.0 C1B A:HEC128 3.1 14.2 1.0 CHD A:HEC128 3.4 14.9 1.0 CHA A:HEC128 3.4 13.5 1.0 CHB A:HEC128 3.4 14.4 1.0 CHC A:HEC128 3.4 14.2 1.0 CD2 A:LEU16 3.8 16.1 1.0 ND1 A:HIS120 4.2 17.3 1.0 CG A:HIS120 4.2 17.7 1.0 NH1 A:ARG124 4.2 26.7 0.7 C2C A:HEC128 4.2 15.3 1.0 C2D A:HEC128 4.3 13.6 1.0 C3D A:HEC128 4.3 13.8 1.0 C2B A:HEC128 4.3 15.9 1.0 C3A A:HEC128 4.3 14.9 1.0 C3C A:HEC128 4.3 14.7 1.0 C3B A:HEC128 4.3 16.3 1.0 C2A A:HEC128 4.3 15.0 1.0 CD1 A:LEU16 4.5 15.9 1.0 NH1 A:ARG124 4.5 20.2 0.3 CG A:LEU16 4.6 14.6 1.0 CB A:LEU16 4.8 13.7 1.0

D.Kekilli, F.S.Dworkowski, G.Pompidor, M.R.Fuchs, C.R.Andrew, S.Antonyuk, R.W.Strange, R.R.Eady, S.S.Hasnain, M.A.Hough. Fingerprinting Redox and Ligand States in Haemprotein Crystal Structures Using Resonance Raman Spectroscopy. Acta Crystallogr.,Sect.D V. 70 1289 2014.
ISSN: ISSN 0907-4449
PubMed: 24816098
DOI: 10.1107/S1399004714004039