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Iron in PDB 1xme: Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus

Enzymatic activity of Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus

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

Protein crystallography data

The structure of Structure of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus, PDB code: 1xme was solved by L.M.Hunsicker-Wang, R.L.Pacoma, Y.Chen, J.A.Fee, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.42 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 114.902, 114.902, 177.064, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 23.6

Other elements in 1xme:

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

Copper (Cu) 3 atoms

Iron Binding Sites:

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

Iron binding site 1 out of 2 in 1xme

Go back to Iron Binding Sites List in 1xme
Iron binding site 1 out of 2 in the Structure of Recombinant 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe800

b:36.8
occ:1.00
FE A:HEM800 0.0 36.8 1.0
ND A:HEM800 2.0 38.1 1.0
NA A:HEM800 2.1 39.8 1.0
NB A:HEM800 2.1 41.1 1.0
NC A:HEM800 2.1 40.0 1.0
NE2 A:HIS72 2.2 29.8 1.0
NE2 A:HIS386 2.2 34.6 1.0
C1D A:HEM800 3.1 37.1 1.0
C4C A:HEM800 3.1 39.8 1.0
C4D A:HEM800 3.1 38.3 1.0
C1A A:HEM800 3.1 38.7 1.0
CD2 A:HIS72 3.1 32.5 1.0
C4B A:HEM800 3.1 41.5 1.0
C1C A:HEM800 3.1 41.3 1.0
C1B A:HEM800 3.1 41.1 1.0
C4A A:HEM800 3.1 38.5 1.0
CD2 A:HIS386 3.1 35.2 1.0
CE1 A:HIS72 3.2 32.4 1.0
CE1 A:HIS386 3.2 37.0 1.0
CHD A:HEM800 3.4 38.6 1.0
CHA A:HEM800 3.4 38.4 1.0
CHC A:HEM800 3.4 41.1 1.0
CHB A:HEM800 3.5 39.6 1.0
C2D A:HEM800 4.2 37.8 1.0
CG A:HIS72 4.3 34.8 1.0
ND1 A:HIS72 4.3 34.5 1.0
C3D A:HEM800 4.3 36.5 1.0
ND1 A:HIS386 4.3 36.4 1.0
CG A:HIS386 4.3 37.2 1.0
C3B A:HEM800 4.3 40.8 1.0
C3C A:HEM800 4.3 41.5 1.0
C2C A:HEM800 4.3 41.0 1.0
C2B A:HEM800 4.4 41.0 1.0
C3A A:HEM800 4.4 41.2 1.0
C2A A:HEM800 4.4 39.4 1.0
NE2 A:GLN42 4.4 46.8 1.0

Iron binding site 2 out of 2 in 1xme

Go back to Iron Binding Sites List in 1xme
Iron binding site 2 out of 2 in the Structure of Recombinant 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 Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:39.9
occ:1.00
FE A:HAS801 0.0 39.9 1.0
ND A:HAS801 2.0 38.9 1.0
NB A:HAS801 2.0 39.4 1.0
NC A:HAS801 2.0 39.3 1.0
NA A:HAS801 2.0 37.6 1.0
O A:HOH867 2.4 29.2 1.0
NE2 A:HIS384 2.5 43.5 1.0
C1D A:HAS801 3.0 39.4 1.0
C4D A:HAS801 3.0 38.6 1.0
C4B A:HAS801 3.0 38.1 1.0
C1C A:HAS801 3.0 38.2 1.0
C1A A:HAS801 3.1 35.0 1.0
C1B A:HAS801 3.1 39.1 1.0
C4C A:HAS801 3.1 38.2 1.0
C4A A:HAS801 3.1 36.1 1.0
CHB A:HAS801 3.4 39.2 1.0
CHA A:HAS801 3.4 35.6 1.0
CD2 A:HIS384 3.4 43.4 1.0
CHC A:HAS801 3.4 37.1 1.0
CHD A:HAS801 3.4 37.1 1.0
CE1 A:HIS384 3.5 46.9 1.0
C3D A:HAS801 4.2 40.4 1.0
C2D A:HAS801 4.3 41.0 1.0
C2B A:HAS801 4.3 39.3 1.0
C3B A:HAS801 4.3 40.4 1.0
C2C A:HAS801 4.3 37.9 1.0
C3C A:HAS801 4.3 37.2 1.0
C3A A:HAS801 4.4 35.7 1.0
C2A A:HAS801 4.4 35.2 1.0
CU A:CU803 4.4 38.5 1.0
ND1 A:HIS384 4.6 44.2 1.0
CG A:HIS384 4.6 43.5 1.0
CE1 A:HIS233 4.9 34.0 1.0

Reference:

L.M.Hunsicker-Wang, R.L.Pacoma, Y.Chen, J.A.Fee, C.D.Stout. A Novel Cryoprotection Scheme For Enhancing the Diffraction of Crystals of Recombinant Cytochrome BA3 Oxidase From Thermus Thermophilus. Acta Crystallogr.,Sect.D V. 61 340 2005.
ISSN: ISSN 0907-4449
PubMed: 15735345
DOI: 10.1107/S0907444904033906
Page generated: Sun Dec 13 14:35:59 2020

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