Iron in PDB 2xl6: Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No, PDB code: 2xl6 was solved by M.A.Hough, S.V.Antonyuk, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.83 / 1.07
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	52.940, 52.940, 182.910, 90.00, 90.00, 120.00
R / Rfree (%)	13.621 / 16.062

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No (pdb code 2xl6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No, PDB code: 2xl6:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No


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: Ferrous R124A Variant with Bound No within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:5.6 occ:0.70 FE A:HEC128 0.0 5.6 0.7 NC A:HEC128 0.9 6.7 0.3 C4C A:HEC128 1.5 6.2 0.3 FE A:HEC128 1.6 6.6 0.3 N A:NO155 1.8 8.6 0.3 N A:NO155 1.8 5.9 0.3 NC A:HEC128 2.0 5.4 0.7 NB A:HEC128 2.0 5.3 0.7 ND A:HEC128 2.0 6.4 0.7 NA A:HEC128 2.0 7.1 0.7 ND A:HEC128 2.1 7.0 0.3 C1C A:HEC128 2.1 4.9 0.3 CHD A:HEC128 2.2 5.6 0.3 N A:NO155 2.3 9.3 0.4 C1D A:HEC128 2.4 7.4 0.3 O A:NO155 2.7 10.5 0.3 C3C A:HEC128 2.7 5.7 0.3 O A:NO155 2.9 8.3 0.3 C2C A:HEC128 2.9 4.0 0.3 NB A:HEC128 3.0 6.3 0.3 C1B A:HEC128 3.0 6.9 0.7 C4B A:HEC128 3.0 4.3 0.7 C4C A:HEC128 3.0 5.7 0.7 C1C A:HEC128 3.0 4.6 0.7 C4D A:HEC128 3.1 8.1 0.7 C1D A:HEC128 3.1 6.7 0.7 C4A A:HEC128 3.1 7.1 0.7 CHC A:HEC128 3.1 5.5 0.3 C1A A:HEC128 3.1 6.8 0.7 O A:NO155 3.2 9.4 0.4 C4B A:HEC128 3.4 5.9 0.3 CHD A:HEC128 3.4 6.2 0.7 CHB A:HEC128 3.4 7.5 0.7 CHC A:HEC128 3.4 5.0 0.7 CHA A:HEC128 3.4 7.5 0.7 C4D A:HEC128 3.5 7.9 0.3 NA A:HEC128 3.5 8.6 0.3 CD2 A:LEU16 3.8 9.6 1.0 C2D A:HEC128 3.8 8.3 0.3 CAC A:HEC128 4.1 6.7 0.3 CB A:HIS120 4.1 8.4 0.5 CA A:HIS120 4.2 7.3 0.3 C3B A:HEC128 4.2 6.0 0.7 C2B A:HEC128 4.3 7.1 0.7 C3C A:HEC128 4.3 5.0 0.7 C1B A:HEC128 4.3 6.2 0.3 C2D A:HEC128 4.3 8.6 0.7 C2C A:HEC128 4.3 5.6 0.7 C3D A:HEC128 4.3 8.9 0.7 CG A:HIS120 4.3 9.2 0.3 CHA A:HEC128 4.3 8.7 0.3 C3A A:HEC128 4.3 7.7 0.7 C2A A:HEC128 4.3 8.2 0.7 C3D A:HEC128 4.3 8.3 0.3 C1A A:HEC128 4.3 9.2 0.3 CMC A:HEC128 4.4 7.0 0.3 CD2 A:HIS120 4.4 10.8 0.3 ND1 A:HIS120 4.5 11.1 0.3 CD1 A:LEU16 4.5 10.2 1.0 N A:HIS120 4.6 6.5 0.3 CG A:LEU16 4.6 8.1 1.0 C4A A:HEC128 4.6 7.7 0.3 C3B A:HEC128 4.8 7.2 0.3 CBC A:HEC128 4.8 6.6 0.3 CHB A:HEC128 4.9 7.1 0.3 CB A:LEU16 4.9 7.1 1.0 CMD A:HEC128 4.9 9.5 0.3 CB A:HIS120 5.0 11.8 0.5

Iron binding site 2 out of 2 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C Prime From Alcaligenes Xylosoxidans: Ferrous R124A Variant with Bound No within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:6.6 occ:0.30 FE A:HEC128 0.0 6.6 0.3 NA A:HEC128 1.2 7.1 0.7 FE A:HEC128 1.6 5.6 0.7 C4A A:HEC128 1.8 7.1 0.7 N A:NO155 1.8 5.9 0.3 N A:NO155 1.9 9.3 0.4 NB A:HEC128 1.9 5.3 0.7 NA A:HEC128 2.0 8.6 0.3 NB A:HEC128 2.0 6.3 0.3 NC A:HEC128 2.0 6.7 0.3 ND A:HEC128 2.0 7.0 0.3 N A:NO155 2.1 8.6 0.3 CHB A:HEC128 2.1 7.5 0.7 C1B A:HEC128 2.2 6.9 0.7 O A:NO155 2.5 8.3 0.3 C1A A:HEC128 2.5 6.8 0.7 C4B A:HEC128 3.0 5.9 0.3 C4A A:HEC128 3.0 7.7 0.3 O A:NO155 3.0 9.4 0.4 C1A A:HEC128 3.0 9.2 0.3 C1B A:HEC128 3.0 6.2 0.3 C4C A:HEC128 3.0 6.2 0.3 C1C A:HEC128 3.0 4.9 0.3 C1D A:HEC128 3.1 7.4 0.3 C4D A:HEC128 3.1 7.9 0.3 C3A A:HEC128 3.1 7.7 0.7 ND A:HEC128 3.1 6.4 0.7 O A:NO155 3.3 10.5 0.3 C4B A:HEC128 3.3 4.3 0.7 CHB A:HEC128 3.4 7.1 0.3 C2A A:HEC128 3.4 8.2 0.7 CHA A:HEC128 3.4 8.7 0.3 CHC A:HEC128 3.4 5.5 0.3 CHA A:HEC128 3.4 7.5 0.7 CHD A:HEC128 3.4 5.6 0.3 NC A:HEC128 3.5 5.4 0.7 C2B A:HEC128 3.6 7.1 0.7 C4D A:HEC128 3.6 8.1 0.7 CG A:HIS120 3.7 9.2 0.3 CD2 A:HIS120 3.9 10.8 0.3 CB A:HIS120 3.9 8.4 0.5 C3B A:HEC128 4.0 6.0 0.7 ND1 A:HIS120 4.1 9.6 0.3 CHC A:HEC128 4.1 5.0 0.7 ND1 A:HIS120 4.2 11.1 0.3 C3B A:HEC128 4.2 7.2 0.3 C3A A:HEC128 4.2 9.1 0.3 C3C A:HEC128 4.2 5.7 0.3 C2C A:HEC128 4.2 4.0 0.3 C2B A:HEC128 4.2 8.2 0.3 C1C A:HEC128 4.2 4.6 0.7 C2A A:HEC128 4.2 9.8 0.3 C2D A:HEC128 4.3 8.3 0.3 C3D A:HEC128 4.3 8.3 0.3 NE2 A:HIS120 4.3 11.7 0.3 CMA A:HEC128 4.4 9.2 0.7 C1D A:HEC128 4.4 6.7 0.7 CE1 A:HIS120 4.4 10.6 0.3 O A:HOH2348 4.5 19.5 0.3 O1D A:HEC128 4.5 18.7 0.3 C4C A:HEC128 4.6 5.7 0.7 CA A:HIS120 4.6 7.3 0.3 CD2 A:LEU16 4.6 9.6 1.0 CMB A:HEC128 4.7 10.3 0.7 CAA A:HEC128 4.9 10.0 0.7 CHD A:HEC128 4.9 6.2 0.7 CG A:HIS120 5.0 11.0 0.3 CE1 A:HIS120 5.0 8.9 0.3

M.A.Hough, S.V.Antonyuk, S.Barbieri, N.Rustage, A.L.Mckay, A.E.Servid, R.R.Eady, C.R.Andrew, S.S.Hasnain. Distal-to-Proximal No Conversion in Hemoproteins: the Role of the Proximal Pocket. J.Mol.Biol. V. 405 395 2011.
ISSN: ISSN 0022-2836
PubMed: 21073879
DOI: 10.1016/J.JMB.2010.10.035