Iron in PDB 2nvf: Soluble Domain of Rieske Iron-Sulfur Protein.

All present enzymatic activity of Soluble Domain of Rieske Iron-Sulfur Protein.:
1.10.2.2;

The structure of Soluble Domain of Rieske Iron-Sulfur Protein., PDB code: 2nvf was solved by D.Kolling, J.Brunzelle, S.Lhee, A.R.Crofts, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.00 / 1.50
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	70.880, 70.880, 54.925, 90.00, 90.00, 90.00
R / Rfree (%)	13.2 / 17.9

The binding sites of Iron atom in the Soluble Domain of Rieske Iron-Sulfur Protein. (pdb code 2nvf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Soluble Domain of Rieske Iron-Sulfur Protein., PDB code: 2nvf:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Soluble Domain of Rieske Iron-Sulfur Protein.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Soluble Domain of Rieske Iron-Sulfur Protein. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:14.0 occ:1.00 FE1 A:FES200 0.0 14.0 1.0 S1 A:FES200 2.2 14.7 1.0 S2 A:FES200 2.2 14.2 1.0 SG A:CYS149 2.3 14.9 1.0 SG A:CYS129 2.3 11.5 1.0 FE2 A:FES200 2.7 15.8 1.0 CB A:CYS129 3.1 10.9 1.0 CB A:CYS149 3.2 13.9 1.0 CB A:HIS131 4.1 14.4 1.0 SG A:CYS154 4.3 24.0 1.0 CB A:CYS134 4.3 15.4 1.0 CB A:CYS151 4.4 18.0 1.0 ND1 A:HIS131 4.4 16.2 1.0 CA A:CYS149 4.5 14.2 1.0 ND1 A:HIS152 4.5 18.6 1.0 CB A:CYS154 4.6 15.0 1.0 N A:HIS152 4.6 16.9 1.0 CA A:CYS129 4.6 10.6 1.0 O A:CYS149 4.7 15.3 1.0 N A:LEU132 4.7 15.8 1.0 C A:CYS149 4.8 15.3 1.0 CG A:HIS131 4.8 14.4 1.0 N A:CYS134 4.8 15.0 1.0 N A:CYS151 5.0 17.9 1.0

Iron binding site 2 out of 2 in the Soluble Domain of Rieske Iron-Sulfur Protein.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Soluble Domain of Rieske Iron-Sulfur Protein. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:15.8 occ:1.00 FE2 A:FES200 0.0 15.8 1.0 ND1 A:HIS152 2.2 18.6 1.0 ND1 A:HIS131 2.2 16.2 1.0 S2 A:FES200 2.2 14.2 1.0 S1 A:FES200 2.2 14.7 1.0 FE1 A:FES200 2.7 14.0 1.0 CE1 A:HIS152 3.1 19.3 1.0 CG A:HIS152 3.1 17.2 1.0 CG A:HIS131 3.1 14.4 1.0 CE1 A:HIS131 3.2 16.9 1.0 CB A:HIS131 3.4 14.4 1.0 CB A:HIS152 3.4 16.9 1.0 N A:HIS152 3.8 16.9 1.0 N A:LEU132 4.1 15.8 1.0 CA A:HIS152 4.1 16.8 1.0 CB A:CYS151 4.1 18.0 1.0 NE2 A:HIS152 4.2 19.4 1.0 CD2 A:HIS152 4.3 19.1 1.0 NE2 A:HIS131 4.3 17.5 1.0 CD2 A:HIS131 4.3 17.0 1.0 SG A:CYS129 4.4 11.5 1.0 C A:CYS151 4.4 17.8 1.0 CB A:LEU132 4.5 16.8 1.0 SG A:CYS149 4.6 14.9 1.0 CG A:PRO166 4.6 15.8 1.0 CA A:HIS131 4.7 14.7 1.0 C A:HIS131 4.8 15.4 1.0 SG A:CYS154 4.8 24.0 1.0 C A:HIS152 4.8 16.7 1.0 CA A:CYS151 4.8 18.3 1.0 CA A:LEU132 4.9 16.4 1.0 CG A:LEU132 4.9 17.6 1.0

D.J.Kolling, J.S.Brunzelle, S.Lhee, A.R.Crofts, S.K.Nair. Atomic Resolution Structures of Rieske Iron-Sulfur Protein: Role of Hydrogen Bonds in Tuning the Redox Potential of Iron-Sulfur Clusters. Structure V. 15 29 2007.
ISSN: ISSN 0969-2126
PubMed: 17223530
DOI: 10.1016/J.STR.2006.11.012