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Iron in PDB 1h1o: Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer

Protein crystallography data

The structure of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer, PDB code: 1h1o was solved by C.Abergel, W.Nitschke, G.Malarte, M.Bruschi, J.-M.Claverie, M.-T.Guidici-Orticoni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25 / 2.13
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 100.049, 100.049, 149.668, 90.00, 90.00, 120.00
R / Rfree (%) 23.9 / 28.4

Other elements in 1h1o:

The structure of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer (pdb code 1h1o). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer, PDB code: 1h1o:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1h1o

Go back to Iron Binding Sites List in 1h1o
Iron binding site 1 out of 4 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1184

b:31.9
occ:1.00
FE A:HEM1184 0.0 31.9 1.0
NB A:HEM1184 1.9 29.4 1.0
ND A:HEM1184 2.0 29.6 1.0
NC A:HEM1184 2.0 32.5 1.0
NA A:HEM1184 2.0 31.0 1.0
NE2 A:HIS123 2.1 31.0 1.0
SD A:MET161 2.3 32.1 1.0
C4B A:HEM1184 3.0 30.9 1.0
C4D A:HEM1184 3.0 32.8 1.0
C1B A:HEM1184 3.0 31.5 1.0
C4C A:HEM1184 3.0 32.2 1.0
C1D A:HEM1184 3.0 34.0 1.0
C1C A:HEM1184 3.0 30.7 1.0
C1A A:HEM1184 3.0 28.3 1.0
C4A A:HEM1184 3.1 30.6 1.0
CD2 A:HIS123 3.1 32.9 1.0
CE1 A:HIS123 3.2 31.1 1.0
CHC A:HEM1184 3.4 29.6 1.0
CHA A:HEM1184 3.4 29.4 1.0
CHD A:HEM1184 3.4 33.1 1.0
CE A:MET161 3.4 32.8 1.0
CG A:MET161 3.4 32.1 1.0
CHB A:HEM1184 3.4 28.0 1.0
C3B A:HEM1184 4.2 29.6 1.0
C3C A:HEM1184 4.2 32.8 1.0
CG A:HIS123 4.2 35.8 1.0
C2B A:HEM1184 4.2 27.9 1.0
ND1 A:HIS123 4.2 32.8 1.0
C2C A:HEM1184 4.3 32.2 1.0
C3D A:HEM1184 4.3 33.0 1.0
C2A A:HEM1184 4.3 30.0 1.0
C2D A:HEM1184 4.3 32.5 1.0
C3A A:HEM1184 4.3 29.4 1.0
CB A:MET161 4.8 33.4 1.0
CD1 A:LEU136 4.9 29.3 1.0

Iron binding site 2 out of 4 in 1h1o

Go back to Iron Binding Sites List in 1h1o
Iron binding site 2 out of 4 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1185

b:36.3
occ:1.00
FE A:HEM1185 0.0 36.3 1.0
ND A:HEM1185 2.0 33.8 1.0
NB A:HEM1185 2.0 37.9 1.0
NC A:HEM1185 2.0 38.9 1.0
NA A:HEM1185 2.0 36.7 1.0
NE2 A:HIS20 2.0 35.6 1.0
SD A:MET64 2.2 38.6 1.0
CE1 A:HIS20 2.9 37.4 1.0
C4D A:HEM1185 3.0 35.4 1.0
C1D A:HEM1185 3.0 36.2 1.0
C4B A:HEM1185 3.0 39.5 1.0
C4C A:HEM1185 3.0 37.5 1.0
C1B A:HEM1185 3.0 37.9 1.0
C1C A:HEM1185 3.0 37.7 1.0
C1A A:HEM1185 3.1 33.7 1.0
C4A A:HEM1185 3.1 37.4 1.0
CD2 A:HIS20 3.2 37.1 1.0
CHD A:HEM1185 3.4 36.9 1.0
CHC A:HEM1185 3.4 39.9 1.0
CHA A:HEM1185 3.4 34.8 1.0
CHB A:HEM1185 3.4 35.8 1.0
CE A:MET64 3.4 39.1 1.0
CG A:MET64 3.5 38.3 1.0
ND1 A:HIS20 4.1 37.3 1.0
CG A:HIS20 4.2 37.3 1.0
C3D A:HEM1185 4.2 33.9 1.0
C3C A:HEM1185 4.2 39.3 1.0
C2D A:HEM1185 4.3 33.9 1.0
C3B A:HEM1185 4.3 40.1 1.0
C2B A:HEM1185 4.3 39.4 1.0
C2C A:HEM1185 4.3 39.5 1.0
C2A A:HEM1185 4.3 36.0 1.0
C3A A:HEM1185 4.3 35.9 1.0
CB A:MET64 4.8 40.8 1.0
O A:TYR63 4.9 39.3 1.0

Iron binding site 3 out of 4 in 1h1o

Go back to Iron Binding Sites List in 1h1o
Iron binding site 3 out of 4 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1385

b:34.1
occ:1.00
FE B:HEM1385 0.0 34.1 1.0
NB B:HEM1385 2.0 33.2 1.0
ND B:HEM1385 2.0 34.2 1.0
NA B:HEM1385 2.0 34.2 1.0
NC B:HEM1385 2.0 34.3 1.0
NE2 B:HIS323 2.1 35.1 1.0
SD B:MET361 2.5 34.2 1.0
C1B B:HEM1385 3.0 33.9 1.0
C4D B:HEM1385 3.0 34.0 1.0
C1A B:HEM1385 3.0 33.5 1.0
C1D B:HEM1385 3.0 33.3 1.0
CE1 B:HIS323 3.0 34.2 1.0
C4A B:HEM1385 3.0 33.1 1.0
C4B B:HEM1385 3.0 33.5 1.0
C4C B:HEM1385 3.0 33.8 1.0
C1C B:HEM1385 3.1 32.2 1.0
CD2 B:HIS323 3.1 35.3 1.0
CE B:MET361 3.2 32.6 1.0
CHA B:HEM1385 3.4 33.2 1.0
CHD B:HEM1385 3.4 31.5 1.0
CHB B:HEM1385 3.4 31.6 1.0
CHC B:HEM1385 3.4 32.4 1.0
CG B:MET361 3.5 35.6 1.0
ND1 B:HIS323 4.2 34.9 1.0
CG B:HIS323 4.2 35.7 1.0
C2B B:HEM1385 4.2 32.5 1.0
C3B B:HEM1385 4.2 33.5 1.0
C2A B:HEM1385 4.2 32.8 1.0
C3C B:HEM1385 4.3 33.6 1.0
C3A B:HEM1385 4.3 34.9 1.0
C3D B:HEM1385 4.3 34.5 1.0
C2D B:HEM1385 4.3 33.8 1.0
C2C B:HEM1385 4.3 32.9 1.0
CB B:MET361 4.8 38.8 1.0
CD1 B:LEU336 4.9 27.2 1.0

Iron binding site 4 out of 4 in 1h1o

Go back to Iron Binding Sites List in 1h1o
Iron binding site 4 out of 4 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1386

b:39.5
occ:1.00
FE B:HEM1386 0.0 39.5 1.0
ND B:HEM1386 2.0 40.1 1.0
NB B:HEM1386 2.0 38.0 1.0
NC B:HEM1386 2.0 40.9 1.0
NA B:HEM1386 2.0 40.0 1.0
NE2 B:HIS220 2.1 43.3 1.0
SD B:MET264 2.3 37.2 1.0
C4D B:HEM1386 3.0 41.3 1.0
CE1 B:HIS220 3.0 44.4 1.0
C1D B:HEM1386 3.0 40.9 1.0
C1B B:HEM1386 3.0 40.7 1.0
C4B B:HEM1386 3.0 41.0 1.0
C1A B:HEM1386 3.0 38.7 1.0
C4C B:HEM1386 3.0 39.7 1.0
C4A B:HEM1386 3.1 38.5 1.0
C1C B:HEM1386 3.1 40.9 1.0
CD2 B:HIS220 3.1 46.0 1.0
CHA B:HEM1386 3.4 39.0 1.0
CHD B:HEM1386 3.4 41.1 1.0
CHC B:HEM1386 3.4 40.6 1.0
CHB B:HEM1386 3.4 39.9 1.0
CG B:MET264 3.5 37.6 1.0
CE B:MET264 3.6 36.8 1.0
ND1 B:HIS220 4.1 44.4 1.0
CG B:HIS220 4.2 47.6 1.0
C3D B:HEM1386 4.2 39.6 1.0
C2B B:HEM1386 4.3 40.0 1.0
C2D B:HEM1386 4.3 41.3 1.0
C3B B:HEM1386 4.3 40.5 1.0
C3C B:HEM1386 4.3 42.0 1.0
C2A B:HEM1386 4.3 39.0 1.0
C3A B:HEM1386 4.3 39.4 1.0
C2C B:HEM1386 4.3 41.6 1.0
CB B:MET264 4.8 40.2 1.0

Reference:

C.Abergel, W.Nitschke, G.Malarte, M.Bruschi, J.-M.Claverie, M.-T.Guidici-Orticoni. The Structure of Acidithiobacillus Ferrooxidans C(4)-Cytochrome. A Model For Complex-Induced Electron Transfer Tuning Structure V. 11 547 2003.
ISSN: ISSN 0969-2126
PubMed: 12737820
DOI: 10.1016/S0969-2126(03)00072-8
Page generated: Sat Aug 3 06:47:36 2024

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