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Iron in PDB 1xln: Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida

Enzymatic activity of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida

All present enzymatic activity of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida:
1.9.3.2;

Protein crystallography data

The structure of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida, PDB code: 1xln was solved by I.F.Sevrioukova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.96 / 2.03
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 50.166, 75.449, 107.859, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida (pdb code 1xln). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida, PDB code: 1xln:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1xln

Go back to Iron Binding Sites List in 1xln
Iron binding site 1 out of 4 in the Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe107

b:27.4
occ:1.00
 FE1 A:FES107 0.0 27.4 1.0
S1 A:FES107 2.2 25.3 1.0
S2 A:FES107 2.2 23.2 1.0
SG A:CYS39 2.3 22.2 1.0
SG A:CYS45 2.3 26.7 1.0
FE2 A:FES107 2.7 26.5 1.0
CB A:CYS39 3.3 27.6 1.0
CB A:CYS45 3.6 28.6 1.0
N A:CYS45 3.6 30.3 1.0
N A:CYS39 3.7 31.1 1.0
CA A:CYS45 4.0 29.3 1.0
CA A:CYS39 4.0 28.9 1.0
N A:SER44 4.1 31.0 1.0
N A:GLY41 4.1 27.3 1.0
C A:CYS45 4.1 29.3 1.0
O A:CYS45 4.2 29.9 1.0
N A:GLY40 4.4 28.8 1.0
C A:CYS39 4.4 29.2 1.0
SG A:CYS86 4.4 20.8 1.0
N A:ALA43 4.5 25.6 1.0
SG A:CYS48 4.5 20.5 1.0
C A:SER44 4.5 31.6 1.0
CA A:GLY41 4.5 24.1 1.0
N A:ASP38 4.6 33.4 1.0
CA A:GLY37 4.6 33.8 1.0
CA A:ALA43 4.7 26.8 1.0
C A:GLY37 4.7 32.9 1.0
N A:ALA46 4.7 28.3 1.0
N A:SER42 4.7 24.6 1.0
CA A:SER44 4.8 33.3 1.0
C A:ALA43 4.8 29.2 1.0
C A:ASP38 4.9 32.8 1.0
C A:GLY41 5.0 24.1 1.0

Iron binding site 2 out of 4 in 1xln

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Iron binding site 2 out of 4 in the Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe107

b:26.5
occ:1.00
 FE2 A:FES107 0.0 26.5 1.0
S1 A:FES107 2.3 25.3 1.0
S2 A:FES107 2.3 23.2 1.0
SG A:CYS48 2.3 20.5 1.0
SG A:CYS86 2.3 20.8 1.0
FE1 A:FES107 2.7 27.4 1.0
CB A:CYS86 3.2 20.1 1.0
CB A:CYS48 3.4 23.1 1.0
N A:CYS86 4.2 18.0 1.0
CA A:CYS86 4.3 19.1 1.0
CA A:GLY41 4.4 24.1 1.0
CB A:LEU84 4.4 26.2 1.0
SG A:CYS39 4.5 22.2 1.0
SG A:CYS45 4.5 26.7 1.0
CA A:CYS48 4.7 23.9 1.0
N A:ALA43 4.7 25.6 1.0
N A:GLY41 4.7 27.3 1.0
N A:CYS48 4.7 25.7 1.0
CA A:ALA43 4.8 26.8 1.0
C A:GLY41 4.9 24.1 1.0
CD1 A:LEU84 4.9 26.1 1.0
O A:CYS45 5.0 29.9 1.0
CD2 A:LEU84 5.0 26.9 1.0

Iron binding site 3 out of 4 in 1xln

Go back to Iron Binding Sites List in 1xln
Iron binding site 3 out of 4 in the Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe107

b:21.0
occ:1.00
 FE1 B:FES107 0.0 21.0 1.0
S1 B:FES107 2.2 14.9 1.0
S2 B:FES107 2.2 16.6 1.0
SG B:CYS45 2.2 18.1 1.0
SG B:CYS39 2.3 19.1 1.0
FE2 B:FES107 2.7 19.2 1.0
CB B:CYS39 3.4 21.1 1.0
CB B:CYS45 3.5 18.7 1.0
N B:CYS45 3.6 18.2 1.0
N B:CYS39 3.8 20.7 1.0
CA B:CYS45 3.9 16.8 1.0
C B:CYS45 4.1 16.6 1.0
CA B:CYS39 4.1 20.2 1.0
N B:SER44 4.1 20.2 1.0
O B:CYS45 4.1 16.4 1.0
N B:GLY41 4.3 21.6 1.0
SG B:CYS86 4.3 15.8 1.0
SG B:CYS48 4.4 15.0 1.0
C B:SER44 4.5 21.0 1.0
N B:ALA43 4.5 22.0 1.0
C B:CYS39 4.6 20.1 1.0
N B:GLY40 4.6 21.2 1.0
CA B:GLY41 4.6 21.2 1.0
CA B:ALA43 4.7 21.0 1.0
C B:GLY37 4.7 19.6 1.0
N B:ALA46 4.7 16.6 1.0
N B:ASP38 4.8 19.2 1.0
OG1 B:THR47 4.8 16.7 1.0
N B:SER42 4.8 20.3 1.0
CA B:SER44 4.8 19.5 1.0
CA B:GLY37 4.9 19.9 1.0
C B:ALA43 4.9 20.3 1.0
C B:ASP38 4.9 21.0 1.0
N B:THR47 5.0 17.5 1.0

Iron binding site 4 out of 4 in 1xln

Go back to Iron Binding Sites List in 1xln
Iron binding site 4 out of 4 in the Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Oxidized C73S/C85S Putidaredoxin, A [2FE-2S] Ferredoxin From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe107

b:19.2
occ:1.00
 FE2 B:FES107 0.0 19.2 1.0
S1 B:FES107 2.2 14.9 1.0
SG B:CYS48 2.2 15.0 1.0
SG B:CYS86 2.3 15.8 1.0
S2 B:FES107 2.3 16.6 1.0
FE1 B:FES107 2.7 21.0 1.0
CB B:CYS86 3.2 15.9 1.0
CB B:CYS48 3.4 15.8 1.0
N B:CYS86 4.2 15.1 1.0
CA B:CYS86 4.3 16.1 1.0
SG B:CYS45 4.4 18.1 1.0
CB B:LEU84 4.4 17.0 1.0
SG B:CYS39 4.4 19.1 1.0
CA B:GLY41 4.4 21.2 1.0
CD2 B:LEU84 4.5 15.6 1.0
CA B:CYS48 4.6 16.9 1.0
N B:CYS48 4.6 16.6 1.0
N B:ALA43 4.7 22.0 1.0
N B:GLY41 4.7 21.6 1.0
CA B:ALA43 4.7 21.0 1.0
CG B:MET24 4.8 18.8 1.0
CG B:LEU84 4.9 18.8 1.0
CD1 B:LEU84 4.9 16.6 1.0
O B:CYS45 4.9 16.4 1.0
C B:GLY41 4.9 22.1 1.0

Reference:

I.F.Sevrioukova, I.F.Sevrioukova. N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 15755454
DOI: 10.1016/J.JMB.2005.01.047
Page generated: Wed Jul 16 22:08:33 2025

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