Iron in PDB 4fxc: Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis

The structure of Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis, PDB code: 4fxc was solved by K.Fukuyama, T.Tsukihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	62.320, 28.510, 108.080, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / n/a

The binding sites of Iron atom in the Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis (pdb code 4fxc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis, PDB code: 4fxc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe99 b:36.8 occ:1.00 FE1 A:FES99 0.0 36.8 1.0 S1 A:FES99 2.2 34.4 1.0 S2 A:FES99 2.2 33.7 1.0 SG A:CYS46 2.3 34.9 1.0 SG A:CYS41 2.3 37.9 1.0 FE2 A:FES99 2.6 26.8 1.0 CB A:CYS46 3.3 34.8 1.0 CB A:CYS41 3.5 37.8 1.0 N A:CYS41 3.5 30.9 1.0 OG A:SER40 3.6 31.6 1.0 N A:ARG42 3.8 33.6 1.0 N A:CYS46 3.9 36.9 1.0 CA A:CYS41 3.9 34.0 1.0 CA A:CYS46 3.9 35.4 1.0 C A:CYS46 4.1 36.8 1.0 SG A:CYS79 4.3 32.4 1.0 C A:CYS41 4.4 34.0 1.0 N A:SER47 4.4 38.9 1.0 O A:CYS46 4.5 37.4 1.0 SG A:CYS49 4.5 25.4 1.0 N A:ALA43 4.5 34.8 1.0 N A:SER40 4.5 30.6 1.0 N A:GLY44 4.6 31.8 1.0 C A:SER40 4.7 33.0 1.0 CA A:ARG42 4.7 35.0 1.0 C A:ALA45 4.7 38.0 1.0 CB A:SER40 4.8 30.6 1.0 N A:ALA45 4.8 38.1 1.0 CA A:SER40 4.9 31.5 1.0

Iron binding site 2 out of 2 in the Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 Angstroms Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe99 b:26.8 occ:1.00 FE2 A:FES99 0.0 26.8 1.0 S2 A:FES99 2.2 33.7 1.0 S1 A:FES99 2.2 34.4 1.0 SG A:CYS49 2.3 25.4 1.0 SG A:CYS79 2.3 32.4 1.0 FE1 A:FES99 2.6 36.8 1.0 CB A:CYS79 3.3 30.2 1.0 CB A:CYS49 3.4 28.1 1.0 O A:LEU77 3.6 32.7 1.0 SG A:CYS41 4.2 37.9 1.0 O A:CYS49 4.3 43.1 1.0 SG A:CYS46 4.4 34.9 1.0 CA A:CYS79 4.5 33.8 1.0 N A:CYS79 4.5 33.0 1.0 N A:ARG42 4.5 33.6 1.0 CA A:CYS49 4.5 36.4 1.0 N A:CYS49 4.6 35.3 1.0 CA A:ARG42 4.6 35.0 1.0 C A:LEU77 4.7 30.4 1.0 CB A:LEU77 4.7 28.6 1.0 N A:GLY44 4.8 31.8 1.0 N A:ALA43 4.8 34.8 1.0 C A:CYS49 4.9 37.6 1.0 CD1 A:LEU77 4.9 25.1 1.0

K.Fukuyama, N.Ueki, H.Nakamura, T.Tsukihara, H.Matsubara. Tertiary Structure of [2FE-2S] Ferredoxin From Spirulina Platensis Refined at 2.5 A Resolution: Structural Comparisons of Plant-Type Ferredoxins and An Electrostatic Potential Analysis. J.Biochem.(Tokyo) V. 117 1017 1995.
ISSN: ISSN 0021-924X
PubMed: 8586613