Iron in PDB 2yli: Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans in Its Ferrous Form at 1.45 A

The structure of Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans in Its Ferrous Form at 1.45 A, PDB code: 2yli was solved by S.V.Antonyuk, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.13 / 1.45
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.266, 53.266, 180.731, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 18.4

The binding sites of Iron atom in the Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans in Its Ferrous Form at 1.45 A (pdb code 2yli). 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 Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans in Its Ferrous Form at 1.45 A, PDB code: 2yli:

Iron binding site 1 out of 1 in the Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans in Its Ferrous Form at 1.45 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans in Its Ferrous Form at 1.45 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:15.6 occ:1.00 FE A:HEC128 0.0 15.6 1.0 NA A:HEC128 2.0 14.8 1.0 ND A:HEC128 2.0 14.8 1.0 NC A:HEC128 2.1 15.5 1.0 NB A:HEC128 2.1 15.2 1.0 NE2 A:HIS120 2.2 16.8 1.0 C1A A:HEC128 3.0 15.6 1.0 C4A A:HEC128 3.1 15.4 1.0 C4C A:HEC128 3.1 14.5 1.0 C1D A:HEC128 3.1 15.0 1.0 C1C A:HEC128 3.1 15.2 1.0 C4D A:HEC128 3.1 14.6 1.0 C1B A:HEC128 3.1 15.8 1.0 C4B A:HEC128 3.1 15.2 1.0 CD2 A:HIS120 3.1 16.5 1.0 CE1 A:HIS120 3.2 17.7 1.0 CHD A:HEC128 3.4 14.4 1.0 CHB A:HEC128 3.4 14.9 1.0 CHA A:HEC128 3.4 15.7 1.0 CHC A:HEC128 3.5 14.7 1.0 CD2 A:LEU16 3.7 15.0 1.0 ND1 A:HIS120 4.3 17.9 1.0 C3A A:HEC128 4.3 14.5 1.0 CG A:HIS120 4.3 17.2 1.0 C3C A:HEC128 4.3 14.6 1.0 C2D A:HEC128 4.3 14.6 1.0 C2A A:HEC128 4.3 15.6 1.0 C2C A:HEC128 4.3 16.2 1.0 C3B A:HEC128 4.3 15.8 1.0 C2B A:HEC128 4.3 17.0 1.0 C3D A:HEC128 4.3 14.8 1.0 NH1 A:ARG124 4.4 23.3 0.7 CD1 A:LEU16 4.4 15.0 1.0 CG A:LEU16 4.5 14.7 1.0 NH1 A:ARG124 4.5 16.8 0.3 CB A:LEU16 4.7 14.7 1.0 CE A:MET19 5.0 16.0 0.3

S.V.Antonyuk, N.Rustage, C.A.Petersen, J.L.Arnst, D.J.Heyes, R.Sharma, N.G.Berry, N.S.Scrutton, R.R.Eady, C.R.Andrew, S.S.Hasnain. Carbon Monoxide Poisoning Is Prevented By the Energy Costs of Conformational Changes in Gas- Binding Haemproteins. Proc.Natl.Acad.Sci.Usa V. 108 15780 2011.
ISSN: ISSN 0027-8424
PubMed: 21900609
DOI: 10.1073/PNAS.1109051108