Iron in PDB 3ztm: Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution: Unrestraint Refinement

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution: Unrestraint Refinement, PDB code: 3ztm 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)	10.00 / 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 (%)	13.3 / n/a

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution: Unrestraint Refinement (pdb code 3ztm). 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: Unrestraint Refinement, PDB code: 3ztm:

Iron binding site 1 out of 1 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: As Isolated L16G Variant at 0.9 A Resolution: Unrestraint 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: Unrestraint 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 1.8 7.4 0.6 O A:HOH2248 2.0 8.0 0.4 NC A:HEC128 2.0 5.4 1.0 ND A:HEC128 2.0 5.8 1.0 NB A:HEC128 2.0 5.6 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 7.2 0.6 CE1 A:HIS120 3.0 7.2 1.0 C1B A:HEC128 3.0 5.8 1.0 C1D A:HEC128 3.0 5.6 1.0 C4B A:HEC128 3.0 5.5 1.0 C1C A:HEC128 3.0 5.5 1.0 C4C A:HEC128 3.0 5.3 1.0 C1A A:HEC128 3.0 6.5 1.0 C4A A:HEC128 3.0 6.2 1.0 C4D A:HEC128 3.1 5.8 1.0 CD2 A:HIS120 3.1 6.5 1.0 CHC A:HEC128 3.4 5.7 1.0 CHD A:HEC128 3.4 5.5 1.0 CHB A:HEC128 3.4 6.2 1.0 CHA A:HEC128 3.4 6.6 1.0 ND1 A:HIS120 4.2 8.2 1.0 CG A:HIS120 4.2 7.5 1.0 C3A A:HEC128 4.3 7.4 1.0 C2D A:HEC128 4.3 5.8 1.0 C2A A:HEC128 4.3 7.1 1.0 C3C A:HEC128 4.3 5.6 1.0 C2C A:HEC128 4.3 5.6 1.0 C3B A:HEC128 4.3 6.1 1.0 C2B A:HEC128 4.3 6.0 1.0 C3D A:HEC128 4.3 6.0 1.0 O A:HOH2048 4.4 12.1 0.4 CE A:MET19 4.6 7.5 0.5 NH1 A:ARG124 4.6 9.9 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