Iron in PDB 2ykz: Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans at 0.84 A Resolution: Restrained Refinement

The structure of Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans at 0.84 A Resolution: Restrained Refinement, PDB code: 2ykz 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)	19.51 / 0.84
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.470, 53.470, 181.190, 90.00, 90.00, 120.00
R / Rfree (%)	10.574 / 11.602

The binding sites of Iron atom in the Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans at 0.84 A Resolution: Restrained Refinement (pdb code 2ykz). 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 at 0.84 A Resolution: Restrained Refinement, PDB code: 2ykz:

Iron binding site 1 out of 1 in the Recombinant Native Cytochrome C Prime From Alcaligenes Xylosoxidans at 0.84 A Resolution: Restrained Refinement


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 at 0.84 A Resolution: Restrained Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:5.3 occ:1.00 FE A:HEC128 0.0 5.3 1.0 NA A:HEC128 2.0 5.7 1.0 NC A:HEC128 2.1 5.5 1.0 ND A:HEC128 2.1 5.5 1.0 NB A:HEC128 2.1 5.9 1.0 NE2 A:HIS120 2.1 6.3 1.0 HD21 A:LEU16 3.0 6.2 1.0 C4A A:HEC128 3.1 6.2 1.0 C1B A:HEC128 3.1 6.7 1.0 C1D A:HEC128 3.1 5.5 1.0 C4B A:HEC128 3.1 6.3 1.0 C1C A:HEC128 3.1 5.7 1.0 C4C A:HEC128 3.1 5.5 1.0 C1A A:HEC128 3.1 5.7 1.0 CD2 A:HIS120 3.1 6.7 1.0 C4D A:HEC128 3.1 5.7 1.0 CE1 A:HIS120 3.1 7.6 1.0 HD2 A:HIS120 3.3 6.8 1.0 HE1 A:HIS120 3.3 7.4 1.0 CHB A:HEC128 3.4 6.8 1.0 CHD A:HEC128 3.4 5.4 1.0 CHC A:HEC128 3.4 6.1 1.0 CHA A:HEC128 3.5 5.8 1.0 HD23 A:LEU16 3.6 6.1 1.0 HD12 A:LEU16 3.6 6.0 1.0 CD2 A:LEU16 3.7 6.4 1.0 HB3 A:LEU16 4.0 5.2 1.0 HH11 A:ARG124 4.0 11.0 1.0 HD2 A:ARG124 4.1 9.3 1.0 ND1 A:HIS120 4.3 8.3 1.0 CG A:HIS120 4.3 7.1 1.0 C3A A:HEC128 4.3 6.5 1.0 C3B A:HEC128 4.3 7.1 1.0 C2B A:HEC128 4.3 8.1 1.0 C2A A:HEC128 4.3 6.2 1.0 C3C A:HEC128 4.3 5.8 1.0 C2C A:HEC128 4.3 5.7 1.0 C2D A:HEC128 4.3 5.5 1.0 C3D A:HEC128 4.3 5.7 1.0 HHB A:HEC128 4.4 6.6 1.0 HHD A:HEC128 4.4 5.4 1.0 HHC A:HEC128 4.4 6.0 1.0 CD1 A:LEU16 4.4 6.1 1.0 HHA A:HEC128 4.4 5.7 1.0 HD22 A:LEU16 4.4 6.2 1.0 CG A:LEU16 4.5 5.4 1.0 NH1 A:ARG124 4.5 11.2 1.0 HH12 A:ARG124 4.7 10.7 1.0 CB A:LEU16 4.7 5.3 1.0 HB3 A:CYS116 4.8 8.1 1.0 HD13 A:LEU16 4.8 6.0 1.0 HH2 A:TRP56 4.8 7.4 1.0 CD A:ARG124 5.0 9.5 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