Iron in PDB 2yld: Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound at 1.25 A

The structure of Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound at 1.25 A, PDB code: 2yld 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)	46.68 / 1.25
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.914, 53.914, 180.864, 90.00, 90.00, 120.00
R / Rfree (%)	16.117 / 19

The binding sites of Iron atom in the Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound at 1.25 A (pdb code 2yld). 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: Carbon Monooxide Bound at 1.25 A, PDB code: 2yld:

Iron binding site 1 out of 1 in the Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound at 1.25 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: Carbon Monooxide Bound at 1.25 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:11.5 occ:1.00 FE A:HEC128 0.0 11.5 1.0 C A:CMO129 1.7 15.4 0.4 C A:CMO129 1.8 28.1 0.6 NA A:HEC128 2.0 12.8 1.0 NE2 A:HIS120 2.0 12.5 1.0 NB A:HEC128 2.0 11.1 1.0 NC A:HEC128 2.0 11.7 1.0 ND A:HEC128 2.1 12.0 1.0 O A:CMO129 2.8 20.1 0.4 O A:CMO129 2.9 18.0 0.6 C4A A:HEC128 3.0 14.6 1.0 CE1 A:HIS120 3.0 13.3 1.0 C1B A:HEC128 3.1 11.5 1.0 C1A A:HEC128 3.1 14.0 1.0 C4C A:HEC128 3.1 10.4 1.0 C1C A:HEC128 3.1 11.0 1.0 CD2 A:HIS120 3.1 11.9 1.0 C4B A:HEC128 3.1 11.7 1.0 C1D A:HEC128 3.1 11.2 1.0 C4D A:HEC128 3.1 12.1 1.0 HE1 A:HIS120 3.2 13.2 1.0 HD2 A:HIS120 3.2 12.1 1.0 CHB A:HEC128 3.4 13.2 1.0 CHD A:HEC128 3.4 11.7 1.0 CHA A:HEC128 3.4 12.5 1.0 CHC A:HEC128 3.4 10.8 1.0 HH11 A:ARG124 4.1 18.6 1.0 ND1 A:HIS120 4.2 13.9 1.0 CG A:HIS120 4.2 13.6 1.0 C3A A:HEC128 4.3 17.2 1.0 C2D A:HEC128 4.3 12.5 1.0 C2B A:HEC128 4.3 11.8 1.0 C2A A:HEC128 4.3 16.9 0.4 C3C A:HEC128 4.3 11.7 1.0 C2A A:HEC128 4.3 15.9 0.6 C2C A:HEC128 4.3 11.2 1.0 C3B A:HEC128 4.3 11.6 1.0 C3D A:HEC128 4.3 12.5 1.0 HD3 A:ARG124 4.3 17.1 1.0 HHB A:HEC128 4.3 13.1 1.0 HHD A:HEC128 4.3 11.4 1.0 HHA A:HEC128 4.4 12.5 1.0 HHC A:HEC128 4.4 11.0 1.0 NH1 A:ARG124 4.5 18.9 1.0 HH2 A:TRP56 4.5 16.9 1.0 HH12 A:ARG124 4.6 18.4 1.0 CD1 A:LEU16 4.6 21.2 0.4 CE A:MET19 4.8 14.0 0.6 HB3 A:CYS116 4.8 12.8 1.0 CD2 A:LEU16 4.9 16.8 0.4 CB A:LEU16 4.9 18.6 0.6 HD1 A:HIS120 4.9 13.4 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