Iron in PDB 4gp5: Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus

All present enzymatic activity of Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus:
1.9.3.1;

The structure of Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus, PDB code: 4gp5 was solved by Y.Li, Y.Chen, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.60 / 2.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	144.090, 97.960, 94.650, 90.00, 127.99, 90.00
R / Rfree (%)	17.3 / 23

The structure of Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Iron atom in the Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus (pdb code 4gp5). 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 Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus, PDB code: 4gp5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W 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 Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:18.1 occ:1.00 FE A:HEM602 0.0 18.1 1.0 NA A:HEM602 2.0 16.1 1.0 NE2 A:HIS72 2.0 16.7 1.0 ND A:HEM602 2.0 15.8 1.0 NC A:HEM602 2.1 16.8 1.0 NE2 A:HIS386 2.2 13.1 1.0 NB A:HEM602 2.2 18.4 1.0 CE1 A:HIS72 2.8 17.0 1.0 C1A A:HEM602 2.9 14.6 1.0 C4D A:HEM602 2.9 15.5 1.0 C1D A:HEM602 3.0 15.2 1.0 C4C A:HEM602 3.0 13.7 1.0 C4A A:HEM602 3.1 16.5 1.0 C4B A:HEM602 3.1 18.6 1.0 C1C A:HEM602 3.1 16.4 1.0 CD2 A:HIS386 3.1 12.0 1.0 CE1 A:HIS386 3.2 12.0 1.0 C1B A:HEM602 3.2 18.7 1.0 CD2 A:HIS72 3.2 14.4 1.0 CHA A:HEM602 3.3 15.5 1.0 CHD A:HEM602 3.3 12.8 1.0 CHC A:HEM602 3.5 17.4 1.0 CHB A:HEM602 3.5 16.8 1.0 ND1 A:HIS72 4.0 17.4 1.0 C3C A:HEM602 4.2 13.6 1.0 CG A:HIS72 4.2 16.4 1.0 C2A A:HEM602 4.2 14.4 1.0 C2C A:HEM602 4.2 14.0 1.0 C3D A:HEM602 4.2 15.6 1.0 C2D A:HEM602 4.2 15.0 1.0 ND1 A:HIS386 4.3 12.1 1.0 C3A A:HEM602 4.3 16.1 1.0 CG A:HIS386 4.3 13.3 1.0 C2B A:HEM602 4.3 19.1 1.0 C3B A:HEM602 4.4 20.6 1.0 OE1 A:GLN42 4.6 18.5 1.0 ND2 A:ASN76 4.9 16.5 1.0

Iron binding site 2 out of 2 in the Structure of Recombinant Cytochrome BA3 Oxidase Mutant Y133W 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 Recombinant Cytochrome BA3 Oxidase Mutant Y133W From Thermus Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe603 b:15.4 occ:1.00 FE A:HAS603 0.0 15.4 1.0 ND A:HAS603 2.0 14.9 1.0 NA A:HAS603 2.0 12.4 1.0 NB A:HAS603 2.0 13.7 1.0 NC A:HAS603 2.0 12.8 1.0 O1 A:PER604 2.1 20.5 1.0 NE2 A:HIS384 2.2 15.8 1.0 C1A A:HAS603 3.0 14.5 1.0 C1B A:HAS603 3.0 13.8 1.0 C4A A:HAS603 3.0 13.3 1.0 C4B A:HAS603 3.0 14.9 1.0 C1C A:HAS603 3.0 14.7 1.0 C4D A:HAS603 3.0 16.7 1.0 C1D A:HAS603 3.1 15.7 1.0 C4C A:HAS603 3.1 13.1 1.0 CD2 A:HIS384 3.1 14.7 1.0 CE1 A:HIS384 3.2 16.8 1.0 O2 A:PER604 3.2 22.2 1.0 CHC A:HAS603 3.4 14.1 1.0 CHB A:HAS603 3.4 13.8 1.0 CHA A:HAS603 3.4 16.2 1.0 CHD A:HAS603 3.4 13.6 1.0 C2C A:HAS603 4.2 15.5 1.0 C2A A:HAS603 4.3 13.8 1.0 CG A:HIS384 4.3 13.1 1.0 C2B A:HAS603 4.3 16.8 1.0 C3D A:HAS603 4.3 17.6 1.0 C3A A:HAS603 4.3 13.0 1.0 C3B A:HAS603 4.3 16.6 1.0 ND1 A:HIS384 4.3 14.2 1.0 C2D A:HAS603 4.4 19.0 1.0 C3C A:HAS603 4.4 15.7 1.0 CU A:CU601 4.8 19.4 1.0 CA A:GLY363 4.9 21.6 1.0 CE1 A:HIS233 5.0 15.2 1.0

W.Mcdonald, C.Funatogawa, Y.Li, I.Szundi, Y.Chen, J.A.Fee, C.D.Stout, O.Einarsdottir. Ligand Access to the Active Site in Thermus Thermophilusba(3) and Bovine Heart Aa(3) Cytochrome Oxidases. Biochemistry V. 52 640 2013.
ISSN: ISSN 0006-2960
PubMed: 23282175
DOI: 10.1021/BI301358A