Iron in PDB 2ylg: Cytochrome C Prime From Alcaligenes Xylosoxidans: Ascorbate and Carbon Monooxide Bound L16A Variant at 1.05 A Resolution

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: Ascorbate and Carbon Monooxide Bound L16A Variant at 1.05 A Resolution, PDB code: 2ylg was solved by S.V.Antonyuk, N.Rustage, 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)	46.45 / 1.05
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.640, 53.640, 181.443, 90.00, 90.00, 120.00
R / Rfree (%)	13.793 / 15.076

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Ascorbate and Carbon Monooxide Bound L16A Variant at 1.05 A Resolution (pdb code 2ylg). 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 Prime From Alcaligenes Xylosoxidans: Ascorbate and Carbon Monooxide Bound L16A Variant at 1.05 A Resolution, PDB code: 2ylg:

Iron binding site 1 out of 1 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Ascorbate and Carbon Monooxide Bound L16A Variant at 1.05 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Prime From Alcaligenes Xylosoxidans: Ascorbate and Carbon Monooxide Bound L16A Variant at 1.05 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:11.7 occ:1.00 FE A:HEC128 0.0 11.7 1.0 C A:CMO129 1.8 12.9 1.0 NC A:HEC128 2.0 11.8 1.0 ND A:HEC128 2.0 12.3 1.0 NB A:HEC128 2.0 11.4 1.0 NA A:HEC128 2.0 12.5 1.0 NE2 A:HIS120 2.1 12.6 1.0 O A:CMO129 3.0 13.8 1.0 C1D A:HEC128 3.0 12.7 1.0 CE1 A:HIS120 3.0 13.5 1.0 C4A A:HEC128 3.0 12.3 1.0 C1C A:HEC128 3.0 11.3 1.0 C1A A:HEC128 3.0 12.7 1.0 C4B A:HEC128 3.0 11.6 1.0 C4C A:HEC128 3.1 12.0 1.0 C1B A:HEC128 3.1 11.8 1.0 C4D A:HEC128 3.1 12.6 1.0 CD2 A:HIS120 3.1 13.0 1.0 HE1 A:HIS120 3.2 13.4 1.0 HD2 A:HIS120 3.3 13.0 1.0 CHC A:HEC128 3.4 11.4 1.0 CHB A:HEC128 3.4 12.0 1.0 CHD A:HEC128 3.4 12.5 1.0 CHA A:HEC128 3.4 12.7 1.0 HB3 A:ALA16 3.9 12.0 1.0 HH11 A:ARG124 4.1 16.1 1.0 ND1 A:HIS120 4.2 13.8 1.0 CG A:HIS120 4.2 13.7 1.0 C2A A:HEC128 4.2 13.4 1.0 C3B A:HEC128 4.3 11.8 1.0 C3C A:HEC128 4.3 12.4 1.0 C2D A:HEC128 4.3 13.3 1.0 C2C A:HEC128 4.3 11.5 1.0 C3A A:HEC128 4.3 13.0 1.0 C2B A:HEC128 4.3 11.6 1.0 C3D A:HEC128 4.3 12.8 1.0 HH2 A:TRP56 4.3 13.5 1.0 HB1 A:ALA16 4.3 12.1 1.0 HHC A:HEC128 4.4 11.4 1.0 HHD A:HEC128 4.4 12.4 1.0 HHB A:HEC128 4.4 11.9 1.0 HHA A:HEC128 4.4 12.5 1.0 HD3 A:ARG124 4.4 16.9 1.0 CB A:ALA16 4.5 12.4 1.0 NH1 A:ARG124 4.6 16.1 1.0 CE A:MET19 4.6 13.0 0.6 HH12 A:ARG124 4.7 16.0 1.0 HD1 A:HIS120 4.9 13.6 1.0 HB3 A:CYS116 5.0 13.7 1.0

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