Iron in PDB 5aur: Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region

Protein crystallography data

The structure of Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region, PDB code: 5aur was solved by C.Ren, S.Nagao, M.Yamanaka, H.Kamikubo, H.Komori, Y.Shomura, Y.Higuchi, S.Hirota, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.26
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 32.850, 42.898, 53.591, 86.73, 86.51, 89.83
R / Rfree (%) 18.1 / 22.9

Other elements in 5aur:

The structure of Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region also contains other interesting chemical elements:

Iodine (I) 11 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region (pdb code 5aur). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region, PDB code: 5aur:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5aur

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Iron binding site 1 out of 4 in the Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe101

b:12.4
occ:1.00
FE A:HEC101 0.0 12.4 1.0
NA A:HEC101 2.0 12.4 1.0
ND A:HEC101 2.0 12.4 1.0
NB A:HEC101 2.0 13.2 1.0
NC A:HEC101 2.1 12.9 1.0
NE2 C:HIS14 2.1 11.7 1.0
SD A:MET62 2.3 15.7 1.0
CE1 C:HIS14 2.9 12.8 1.0
C4A A:HEC101 3.0 13.3 1.0
C4D A:HEC101 3.0 12.7 1.0
C1B A:HEC101 3.0 12.6 1.0
C4B A:HEC101 3.0 11.8 1.0
C1D A:HEC101 3.1 12.4 1.0
C1A A:HEC101 3.1 12.9 1.0
C4C A:HEC101 3.1 12.6 1.0
C1C A:HEC101 3.1 12.6 1.0
CD2 C:HIS14 3.2 13.3 1.0
CHC A:HEC101 3.4 13.1 1.0
CG A:MET62 3.4 14.6 1.0
CHA A:HEC101 3.4 15.1 1.0
CHB A:HEC101 3.4 12.4 1.0
CHD A:HEC101 3.4 11.4 1.0
CE A:MET62 3.5 17.6 1.0
CB A:MET62 4.1 14.0 1.0
ND1 C:HIS14 4.1 12.6 1.0
CG C:HIS14 4.2 11.2 1.0
C3D A:HEC101 4.2 13.2 1.0
C3A A:HEC101 4.2 14.0 1.0
C3B A:HEC101 4.3 12.2 1.0
C2B A:HEC101 4.3 14.1 1.0
C2A A:HEC101 4.3 12.9 1.0
C3C A:HEC101 4.3 12.3 1.0
C2C A:HEC101 4.3 13.0 1.0
C2D A:HEC101 4.3 12.8 1.0

Iron binding site 2 out of 4 in 5aur

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Iron binding site 2 out of 4 in the Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe101

b:13.0
occ:1.00
FE C:HEC101 0.0 13.0 1.0
NC C:HEC101 2.0 12.7 1.0
NB C:HEC101 2.0 13.3 1.0
ND C:HEC101 2.0 12.1 1.0
NE2 A:HIS14 2.0 11.4 1.0
NA C:HEC101 2.1 12.1 1.0
SD C:MET62 2.3 14.2 1.0
CE1 A:HIS14 2.9 11.6 1.0
C4B C:HEC101 3.0 12.7 1.0
C4C C:HEC101 3.0 12.1 1.0
C1C C:HEC101 3.0 13.6 1.0
C1D C:HEC101 3.0 12.2 1.0
C4D C:HEC101 3.0 12.1 1.0
C1B C:HEC101 3.0 11.7 1.0
C1A C:HEC101 3.1 12.3 1.0
C4A C:HEC101 3.1 11.4 1.0
CD2 A:HIS14 3.1 12.3 1.0
CHC C:HEC101 3.4 12.1 1.0
CHD C:HEC101 3.4 12.0 1.0
CHA C:HEC101 3.4 11.7 1.0
CG C:MET62 3.4 12.9 1.0
CHB C:HEC101 3.4 11.4 1.0
CE C:MET62 3.5 14.6 1.0
ND1 A:HIS14 4.1 13.5 1.0
CB C:MET62 4.1 13.6 1.0
CG A:HIS14 4.2 15.1 1.0
C3C C:HEC101 4.2 13.5 1.0
C3B C:HEC101 4.2 13.3 1.0
C2D C:HEC101 4.2 13.4 1.0
C2B C:HEC101 4.2 12.9 1.0
C2C C:HEC101 4.2 14.6 1.0
C3D C:HEC101 4.3 13.9 1.0
C3A C:HEC101 4.3 12.3 1.0
C2A C:HEC101 4.3 12.2 1.0

Iron binding site 3 out of 4 in 5aur

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Iron binding site 3 out of 4 in the Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe101

b:15.7
occ:1.00
FE E:HEC101 0.0 15.7 1.0
NA E:HEC101 2.0 14.9 1.0
ND E:HEC101 2.0 15.1 1.0
NB E:HEC101 2.0 14.3 1.0
NC E:HEC101 2.1 14.8 1.0
NE2 G:HIS14 2.1 14.5 1.0
SD E:MET62 2.3 18.2 1.0
CE1 G:HIS14 2.9 17.1 1.0
C4A E:HEC101 3.0 14.6 1.0
C1A E:HEC101 3.0 16.9 1.0
C1D E:HEC101 3.1 14.2 1.0
C4B E:HEC101 3.1 14.2 1.0
C4C E:HEC101 3.1 13.7 1.0
C4D E:HEC101 3.1 17.5 1.0
C1B E:HEC101 3.1 15.6 1.0
C1C E:HEC101 3.1 15.0 1.0
CD2 G:HIS14 3.2 15.6 1.0
CHD E:HEC101 3.4 14.1 1.0
CHB E:HEC101 3.4 20.5 1.0
CHA E:HEC101 3.4 17.9 1.0
CHC E:HEC101 3.4 14.7 1.0
CG E:MET62 3.4 15.5 1.0
CE E:MET62 3.6 21.9 1.0
ND1 G:HIS14 4.1 16.0 1.0
CB E:MET62 4.1 19.1 1.0
C3A E:HEC101 4.2 17.5 1.0
CG G:HIS14 4.2 14.8 1.0
C2A E:HEC101 4.3 17.5 1.0
C3B E:HEC101 4.3 14.8 1.0
C2D E:HEC101 4.3 16.5 1.0
C2B E:HEC101 4.3 16.2 1.0
C3D E:HEC101 4.3 18.3 1.0
C2C E:HEC101 4.3 14.2 1.0
C3C E:HEC101 4.3 13.1 1.0

Iron binding site 4 out of 4 in 5aur

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Iron binding site 4 out of 4 in the Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Hydrogenobacter Thermophilus Cytochrome C552 Dimer Formed By Domain Swapping at N-Terminal Region within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe101

b:11.9
occ:1.00
FE G:HEC101 0.0 11.9 1.0
ND G:HEC101 2.0 12.1 1.0
NB G:HEC101 2.0 12.3 1.0
NC G:HEC101 2.0 11.7 1.0
NE2 E:HIS14 2.1 11.5 1.0
NA G:HEC101 2.1 12.1 1.0
SD G:MET62 2.3 11.7 0.5
SD G:MET62 2.4 15.4 0.5
CE1 E:HIS14 3.0 11.7 1.0
C4C G:HEC101 3.0 12.6 1.0
C1D G:HEC101 3.0 12.2 1.0
C1B G:HEC101 3.0 11.2 1.0
C4D G:HEC101 3.0 10.2 1.0
C4B G:HEC101 3.1 11.6 1.0
C4A G:HEC101 3.1 11.5 1.0
C1C G:HEC101 3.1 12.3 1.0
C1A G:HEC101 3.1 10.8 1.0
CD2 E:HIS14 3.1 13.5 1.0
CHD G:HEC101 3.4 11.3 1.0
CE G:MET62 3.4 14.2 0.5
CG G:MET62 3.4 16.6 0.5
CHB G:HEC101 3.4 11.3 1.0
CG G:MET62 3.4 11.5 0.5
CHC G:HEC101 3.4 13.1 1.0
CHA G:HEC101 3.4 10.7 1.0
CE G:MET62 3.5 9.3 0.5
CB G:MET62 4.1 12.1 0.5
ND1 E:HIS14 4.1 12.4 1.0
CB G:MET62 4.2 18.7 0.5
C3D G:HEC101 4.2 11.4 1.0
CG E:HIS14 4.2 13.9 1.0
C3C G:HEC101 4.2 12.8 1.0
C3B G:HEC101 4.2 11.2 1.0
C2C G:HEC101 4.3 13.0 1.0
C2B G:HEC101 4.3 11.8 1.0
C2D G:HEC101 4.3 12.2 1.0
C2A G:HEC101 4.3 11.9 1.0
C3A G:HEC101 4.3 13.4 1.0

Reference:

C.Ren, S.Nagao, M.Yamanaka, H.Komori, Y.Shomura, Y.Higuchi, S.Hirota. Oligomerization Enhancement and Two Domain Swapping Mode Detection For Thermostable Cytochrome C552VIA the Elongation of the Major Hinge Loop. Mol Biosyst V. 11 3218 2015.
ISSN: ESSN 1742-2051
PubMed: 26451671
DOI: 10.1039/C5MB00545K
Page generated: Sun Dec 13 15:56:31 2020

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