Iron in PDB 2yl7: Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution - Restraint Refinement

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution - Restraint Refinement, PDB code: 2yl7 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)	46.23 / 0.90
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.377, 53.377, 181.652, 90.00, 90.00, 120.00
R / Rfree (%)	12.401 / 13.96

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution - Restraint Refinement (pdb code 2yl7). 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: As Isolated L16G Variant at 0.9 A Resolution - Restraint Refinement, PDB code: 2yl7:

Iron binding site 1 out of 1 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution - Restraint Refinement


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: As Isolated L16G Variant at 0.9 A Resolution - Restraint Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:5.4 occ:1.00 FE A:HEC128 0.0 5.4 1.0 C A:CMO155 1.9 7.0 0.6 O A:HOH2330 1.9 7.9 0.4 ND A:HEC128 2.0 5.7 1.0 NC A:HEC128 2.0 5.5 1.0 NB A:HEC128 2.0 5.5 1.0 NA A:HEC128 2.0 6.0 1.0 NE2 A:HIS120 2.0 6.2 1.0 O A:CMO155 3.0 7.0 0.6 CE1 A:HIS120 3.0 7.2 1.0 C1D A:HEC128 3.0 5.7 1.0 C4A A:HEC128 3.0 6.0 1.0 C1B A:HEC128 3.0 5.7 1.0 C4B A:HEC128 3.0 5.6 1.0 C1C A:HEC128 3.0 5.6 1.0 C1A A:HEC128 3.0 6.5 1.0 C4C A:HEC128 3.0 5.3 1.0 C4D A:HEC128 3.1 5.8 1.0 CD2 A:HIS120 3.1 6.6 1.0 HE1 A:HIS120 3.2 7.1 1.0 HD2 A:HIS120 3.3 6.6 1.0 CHB A:HEC128 3.4 6.2 1.0 CHD A:HEC128 3.4 5.6 1.0 CHC A:HEC128 3.4 5.7 1.0 CHA A:HEC128 3.4 6.5 1.0 ND1 A:HIS120 4.2 8.1 1.0 HH11 A:ARG124 4.2 9.9 1.0 CG A:HIS120 4.2 7.6 1.0 C3A A:HEC128 4.3 7.2 1.0 C2D A:HEC128 4.3 5.8 1.0 C2A A:HEC128 4.3 7.3 1.0 C2C A:HEC128 4.3 5.7 1.0 C3C A:HEC128 4.3 5.7 1.0 C3B A:HEC128 4.3 6.2 1.0 C2B A:HEC128 4.3 6.0 1.0 C3D A:HEC128 4.3 6.2 1.0 O A:HOH2047 4.3 10.6 0.4 HHC A:HEC128 4.4 5.5 1.0 HHB A:HEC128 4.4 6.1 1.0 HHD A:HEC128 4.4 5.5 1.0 HH2 A:TRP56 4.4 7.2 1.0 HHA A:HEC128 4.4 6.3 1.0 CE A:MET19 4.6 7.3 0.5 HD3 A:ARG124 4.6 9.5 1.0 HA3 A:GLY16 4.6 5.9 1.0 NH1 A:ARG124 4.6 9.8 1.0 HA2 A:GLY16 4.6 5.9 1.0 HH12 A:ARG124 4.6 9.8 1.0 HD1 A:HIS120 4.9 7.6 1.0 HB3 A:CYS116 5.0 8.6 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