Iron in PDB 3eh4: Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus

All present enzymatic activity of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus:
1.9.3.1;

The structure of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 3eh4 was solved by B.Liu, Y.Chen, T.Doukov, S.M.Soltis, D.Stout, J.A.Fee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	120.851, 120.851, 150.397, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 26.8

The structure of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Iron atom in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus (pdb code 3eh4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 3eh4:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:94.4 occ:1.00 FE A:HEM800 0.0 94.4 1.0 NA A:HEM800 1.8 79.6 1.0 NB A:HEM800 1.9 84.5 1.0 ND A:HEM800 2.0 84.0 1.0 NE2 A:HIS72 2.1 0.3 1.0 NE2 A:HIS386 2.2 93.1 1.0 NC A:HEM800 2.2 78.0 1.0 C1A A:HEM800 2.8 85.0 1.0 C4A A:HEM800 2.9 82.4 1.0 C1B A:HEM800 2.9 85.7 1.0 C4D A:HEM800 2.9 89.1 1.0 CE1 A:HIS386 3.0 89.7 1.0 CD2 A:HIS72 3.0 0.0 1.0 C4B A:HEM800 3.1 83.3 1.0 CE1 A:HIS72 3.1 0.6 1.0 C1D A:HEM800 3.2 91.0 1.0 C1C A:HEM800 3.2 85.1 1.0 CHA A:HEM800 3.2 85.6 1.0 CHB A:HEM800 3.3 84.5 1.0 CD2 A:HIS386 3.3 89.2 1.0 C4C A:HEM800 3.4 84.8 1.0 CHC A:HEM800 3.6 78.6 1.0 CHD A:HEM800 3.7 89.2 1.0 C2A A:HEM800 4.1 79.6 1.0 C3A A:HEM800 4.1 80.8 1.0 ND1 A:HIS386 4.1 93.3 1.0 CG A:HIS72 4.1 0.4 1.0 C2B A:HEM800 4.2 90.9 1.0 ND1 A:HIS72 4.2 0.8 1.0 C3D A:HEM800 4.2 91.6 1.0 C3B A:HEM800 4.2 92.6 1.0 CG A:HIS386 4.3 90.2 1.0 C2D A:HEM800 4.3 91.7 1.0 NE2 A:GLN42 4.4 99.6 1.0 C2C A:HEM800 4.4 85.4 1.0 C3C A:HEM800 4.6 82.5 1.0

Iron binding site 2 out of 2 in the Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Reduced Form of Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:94.1 occ:1.00 FE A:HAS801 0.0 94.1 1.0 NC A:HAS801 2.1 94.1 1.0 NB A:HAS801 2.1 91.1 1.0 ND A:HAS801 2.1 88.7 1.0 NA A:HAS801 2.1 92.4 1.0 NE2 A:HIS384 2.4 97.1 1.0 C1D A:HAS801 3.1 91.5 1.0 C4C A:HAS801 3.1 93.8 1.0 C1B A:HAS801 3.1 91.2 1.0 O A:HOH596 3.1 78.0 1.0 C4A A:HAS801 3.1 94.4 1.0 C1C A:HAS801 3.1 94.2 1.0 C1A A:HAS801 3.2 91.7 1.0 C4B A:HAS801 3.2 89.3 1.0 C4D A:HAS801 3.2 89.5 1.0 CE1 A:HIS384 3.3 94.9 1.0 CD2 A:HIS384 3.4 98.5 1.0 CHB A:HAS801 3.4 89.0 1.0 CHD A:HAS801 3.4 93.0 1.0 CHC A:HAS801 3.5 90.4 1.0 CHA A:HAS801 3.6 87.9 1.0 C2D A:HAS801 4.3 93.1 1.0 C2B A:HAS801 4.3 93.1 1.0 C3B A:HAS801 4.4 90.2 1.0 C3C A:HAS801 4.4 92.9 1.0 C3D A:HAS801 4.4 90.4 1.0 C2C A:HAS801 4.4 94.5 1.0 C2A A:HAS801 4.4 92.8 1.0 C3A A:HAS801 4.4 95.3 1.0 ND1 A:HIS384 4.5 87.5 1.0 CG A:HIS384 4.5 92.7 1.0 CU A:CU1803 4.7 98.4 1.0 ND2 A:ASN366 5.0 92.7 1.0

B.Liu, Y.Chen, T.Doukov, S.M.Soltis, C.D.Stout, J.A.Fee. Combined Microspectrophotometric and Crystallographic Examination of Chemically Reduced and X-Ray Radiation-Reduced Forms of Cytochrome BA3 Oxidase From Thermus Thermophilus: Structure of the Reduced Form of the Enzyme. Biochemistry V. 48 820 2009.
ISSN: ISSN 0006-2960
PubMed: 19140675
DOI: 10.1021/BI801759A