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Iron in PDB 3s3b: Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization

Enzymatic activity of Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization

All present enzymatic activity of Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization:
1.9.3.1;

Protein crystallography data

The structure of Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization, PDB code: 3s3b was solved by V.M.Luna, J.A.Fee, A.A.Deniz, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 92.32 / 3.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 109.920, 109.920, 170.110, 90.00, 90.00, 90.00
R / Rfree (%) 25.7 / 29.9

Other elements in 3s3b:

The structure of Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization also contains other interesting chemical elements:

Xenon (Xe) 3 atoms
Copper (Cu) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization (pdb code 3s3b). 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 Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization, PDB code: 3s3b:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3s3b

Go back to Iron Binding Sites List in 3s3b
Iron binding site 1 out of 2 in the Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe800

b:86.3
occ:1.00
FE A:HEM800 0.0 86.3 1.0
NE2 A:HIS386 2.0 86.3 1.0
NC A:HEM800 2.0 86.3 1.0
ND A:HEM800 2.0 86.3 1.0
NB A:HEM800 2.0 86.3 1.0
NA A:HEM800 2.1 86.3 1.0
NE2 A:HIS72 2.3 86.3 1.0
CD2 A:HIS386 2.9 86.3 1.0
CE1 A:HIS386 3.0 86.3 1.0
C4C A:HEM800 3.0 86.3 1.0
C1D A:HEM800 3.0 86.3 1.0
C4D A:HEM800 3.0 86.3 1.0
C1B A:HEM800 3.1 86.3 1.0
C4B A:HEM800 3.1 86.3 1.0
C1C A:HEM800 3.1 86.3 1.0
C4A A:HEM800 3.1 86.3 1.0
C1A A:HEM800 3.1 86.3 1.0
CD2 A:HIS72 3.3 86.3 1.0
CE1 A:HIS72 3.3 86.3 1.0
CHD A:HEM800 3.4 86.3 1.0
CHA A:HEM800 3.4 86.3 1.0
CHB A:HEM800 3.4 86.3 1.0
CHC A:HEM800 3.4 86.3 1.0
ND1 A:HIS386 4.0 86.3 1.0
CG A:HIS386 4.1 86.3 1.0
C3C A:HEM800 4.2 86.3 1.0
C2D A:HEM800 4.3 86.3 1.0
C3D A:HEM800 4.3 86.3 1.0
C2B A:HEM800 4.3 86.3 1.0
C3B A:HEM800 4.3 86.3 1.0
C2C A:HEM800 4.3 86.3 1.0
C3A A:HEM800 4.3 86.3 1.0
C2A A:HEM800 4.3 86.3 1.0
ND1 A:HIS72 4.4 86.3 1.0
CG A:HIS72 4.4 86.3 1.0
NE2 A:GLN42 4.7 86.3 1.0

Iron binding site 2 out of 2 in 3s3b

Go back to Iron Binding Sites List in 3s3b
Iron binding site 2 out of 2 in the Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Thermus Thermophilus Cytochrome BA3 Oxidase 240S After Xe Depressurization within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:86.3
occ:1.00
FE A:HAS801 0.0 86.3 1.0
NC A:HAS801 2.1 86.3 1.0
ND A:HAS801 2.1 86.3 1.0
NB A:HAS801 2.1 86.3 1.0
NA A:HAS801 2.1 86.3 1.0
NE2 A:HIS384 2.4 86.3 1.0
C1D A:HAS801 3.1 86.3 1.0
C1C A:HAS801 3.1 86.3 1.0
C1B A:HAS801 3.1 86.3 1.0
C4D A:HAS801 3.1 86.3 1.0
C1A A:HAS801 3.1 86.3 1.0
C4A A:HAS801 3.1 86.3 1.0
C4B A:HAS801 3.1 86.3 1.0
C4C A:HAS801 3.1 86.3 1.0
CD2 A:HIS384 3.3 86.3 1.0
CE1 A:HIS384 3.4 86.3 1.0
CHB A:HAS801 3.4 86.3 1.0
CHA A:HAS801 3.4 86.3 1.0
CHC A:HAS801 3.5 86.3 1.0
CHD A:HAS801 3.5 86.3 1.0
C2D A:HAS801 4.2 86.3 1.0
C3D A:HAS801 4.3 86.3 1.0
C2B A:HAS801 4.3 86.3 1.0
C3B A:HAS801 4.3 86.3 1.0
C2C A:HAS801 4.4 86.3 1.0
CU A:CU803 4.4 86.3 1.0
C2A A:HAS801 4.4 86.3 1.0
C3A A:HAS801 4.4 86.3 1.0
C3C A:HAS801 4.5 86.3 1.0
ND1 A:HIS384 4.5 86.3 1.0
CG A:HIS384 4.5 86.3 1.0
CE1 A:HIS233 5.0 86.3 1.0

Reference:

V.M.Luna, J.A.Fee, A.A.Deniz, C.D.Stout. Mobility of Xe Atoms Within the Oxygen Diffusion Channel of Cytochrome Ba(3) Oxidase. Biochemistry V. 51 4669 2012.
ISSN: ISSN 0006-2960
PubMed: 22607023
DOI: 10.1021/BI3003988
Page generated: Sun Aug 4 19:49:53 2024

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