Iron in PDB 1cgn: Cytochrome C'

The structure of Cytochrome C', PDB code: 1cgn was solved by A.J.Dobbs, H.R.Faber, B.F.Anderson, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.15
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	54.600, 54.600, 180.400, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Cytochrome C' (pdb code 1cgn). 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', PDB code: 1cgn:

Iron binding site 1 out of 1 in the Cytochrome C'


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C' within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:19.6 occ:1.00 FE A:HEM128 0.0 19.6 1.0 NA A:HEM128 1.9 23.5 1.0 NB A:HEM128 2.0 22.6 1.0 NC A:HEM128 2.0 16.2 1.0 NE2 A:HIS120 2.0 13.8 1.0 ND A:HEM128 2.0 18.3 1.0 CD2 A:HIS120 2.9 16.9 1.0 C4A A:HEM128 3.0 26.8 1.0 C1B A:HEM128 3.0 14.5 1.0 C1A A:HEM128 3.0 20.1 1.0 CE1 A:HIS120 3.1 18.6 1.0 C4B A:HEM128 3.1 16.6 1.0 C1C A:HEM128 3.1 28.1 1.0 C4C A:HEM128 3.1 16.3 1.0 C4D A:HEM128 3.1 19.5 1.0 C1D A:HEM128 3.1 15.4 1.0 CHB A:HEM128 3.3 9.8 1.0 CHD A:HEM128 3.4 18.5 1.0 CHA A:HEM128 3.4 18.4 1.0 CHC A:HEM128 3.5 12.7 1.0 CD2 A:LEU16 3.5 11.1 1.0 CG A:HIS120 4.1 14.8 1.0 ND1 A:HIS120 4.1 15.3 1.0 C3A A:HEM128 4.2 27.7 1.0 C2A A:HEM128 4.2 20.9 1.0 C2B A:HEM128 4.2 25.8 1.0 C3B A:HEM128 4.3 19.8 1.0 C2C A:HEM128 4.3 15.8 1.0 C3D A:HEM128 4.3 18.4 1.0 C2D A:HEM128 4.3 23.1 1.0 C3C A:HEM128 4.3 25.5 1.0 CD1 A:LEU16 4.4 14.9 1.0 CG A:LEU16 4.4 18.1 1.0 CB A:LEU16 4.8 16.7 1.0 NE A:ARG124 4.9 38.6 1.0

A.J.Dobbs, B.F.Anderson, H.R.Faber, E.N.Baker. Three-Dimensional Structure of Cytochrome C' From Two Alcaligenes Species and the Implications For Four-Helix Bundle Structures. Acta Crystallogr.,Sect.D V. 52 356 1996.
ISSN: ISSN 0907-4449
PubMed: 15299707
DOI: 10.1107/S0907444995008328