Iron in PDB 3s8f: 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment

All present enzymatic activity of 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment:
1.9.3.1;

The structure of 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment, PDB code: 3s8f was solved by T.Tiefenbrunn, W.Liu, Y.Chen, V.Katritch, C.D.Stout, J.A.Fee, V.Cherezov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.26 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	143.585, 97.816, 94.952, 90.00, 128.30, 90.00
R / Rfree (%)	18.4 / 21.5

The structure of 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Iron atom in the 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment (pdb code 3s8f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment, PDB code: 3s8f:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:16.8 occ:1.00 FE A:HEM800 0.0 16.8 1.0 NC A:HEM800 1.9 15.3 1.0 NA A:HEM800 1.9 18.6 1.0 NB A:HEM800 2.0 15.2 1.0 ND A:HEM800 2.0 13.7 1.0 NE2 A:HIS386 2.0 14.9 1.0 NE2 A:HIS72 2.1 12.4 1.0 C1D A:HEM800 2.9 15.8 1.0 CE1 A:HIS386 3.0 18.6 1.0 C1B A:HEM800 3.0 15.4 1.0 C4B A:HEM800 3.0 10.4 1.0 C4C A:HEM800 3.0 17.2 1.0 CD2 A:HIS72 3.0 14.2 1.0 C4D A:HEM800 3.0 10.8 1.0 C1A A:HEM800 3.1 14.7 1.0 C4A A:HEM800 3.1 14.7 1.0 CE1 A:HIS72 3.1 20.6 1.0 C1C A:HEM800 3.1 16.3 1.0 CD2 A:HIS386 3.1 14.8 1.0 CHD A:HEM800 3.4 14.1 1.0 CHB A:HEM800 3.5 16.7 1.0 CHC A:HEM800 3.5 13.5 1.0 CHA A:HEM800 3.6 13.8 1.0 ND1 A:HIS386 4.1 16.1 1.0 C2C A:HEM800 4.1 14.5 1.0 C2D A:HEM800 4.1 12.9 1.0 C2B A:HEM800 4.2 16.8 1.0 C3C A:HEM800 4.2 17.6 1.0 ND1 A:HIS72 4.2 15.9 1.0 CG A:HIS72 4.2 17.3 1.0 CG A:HIS386 4.2 17.8 1.0 C3D A:HEM800 4.2 12.2 1.0 C2A A:HEM800 4.2 16.8 1.0 C3A A:HEM800 4.2 20.9 1.0 C3B A:HEM800 4.2 15.6 1.0 OE1 A:GLN42 4.5 23.5 1.0 ND2 A:ASN76 5.0 25.4 1.0

Iron binding site 2 out of 2 in the 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 1.8 A Structure of BA3 Cytochrome C Oxidase From Thermus Thermophilus in Lipid Environment within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:20.4 occ:1.00 FE A:HAS801 0.0 20.4 1.0 ND A:HAS801 1.9 19.5 1.0 NC A:HAS801 2.0 16.4 1.0 NB A:HAS801 2.0 19.7 1.0 NA A:HAS801 2.1 16.1 1.0 NE2 A:HIS384 2.1 17.5 1.0 O1 A:PER563 2.3 21.1 1.0 C4A A:HAS801 3.0 16.7 1.0 C4B A:HAS801 3.0 19.5 1.0 C1B A:HAS801 3.0 15.3 1.0 C4C A:HAS801 3.1 15.7 1.0 CD2 A:HIS384 3.1 20.1 1.0 C1D A:HAS801 3.1 21.9 1.0 C1C A:HAS801 3.1 14.5 1.0 C1A A:HAS801 3.1 14.8 1.0 CE1 A:HIS384 3.1 19.9 1.0 C4D A:HAS801 3.1 20.2 1.0 CHD A:HAS801 3.3 19.7 1.0 CHB A:HAS801 3.4 17.9 1.0 CHC A:HAS801 3.5 21.6 1.0 CHA A:HAS801 3.5 17.3 1.0 O2 A:PER563 3.6 19.4 1.0 ND1 A:HIS384 4.2 19.2 1.0 CG A:HIS384 4.2 16.6 1.0 C2C A:HAS801 4.3 15.7 1.0 C3A A:HAS801 4.3 11.8 1.0 C2B A:HAS801 4.3 20.0 1.0 C3B A:HAS801 4.3 18.2 1.0 C2D A:HAS801 4.3 23.7 1.0 C2A A:HAS801 4.3 15.5 1.0 C3C A:HAS801 4.3 19.5 1.0 C3D A:HAS801 4.4 23.5 1.0 CU A:CU803 4.9 23.0 1.0 ND2 A:ASN366 4.9 22.7 1.0 CA A:GLY363 4.9 21.6 1.0 CE1 A:HIS233 5.0 21.2 1.0 CG2 A:VAL236 5.0 20.9 1.0

T.Tiefenbrunn, W.Liu, Y.Chen, V.Katritch, C.D.Stout, J.A.Fee, V.Cherezov. High Resolution Structure of the BA3 Cytochrome C Oxidase From Thermus Thermophilus in A Lipidic Environment. Plos One V. 6 22348 2011.
ISSN: ESSN 1932-6203
PubMed: 21814577
DOI: 10.1371/JOURNAL.PONE.0022348