Iron in PDB 2nvg: 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: 2nvg 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 / 1.35
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	69.935, 69.935, 54.582, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 15.9

The binding sites of Iron atom in the Soluble Domain of Rieske Iron Sulfur Protein. (pdb code 2nvg). 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: 2nvg:
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:18.2 occ:1.00 FE1 A:FES200 0.0 18.2 1.0 S1 A:FES200 2.2 20.1 1.0 S2 A:FES200 2.2 18.6 1.0 SG A:CYS149 2.3 19.2 1.0 SG A:CYS129 2.3 16.2 1.0 FE2 A:FES200 2.7 19.9 1.0 CB A:CYS129 3.1 15.2 1.0 CB A:CYS149 3.2 19.0 1.0 CB A:HIS131 4.1 18.8 1.0 CB A:CYS151 4.3 22.8 1.0 ND1 A:HIS131 4.3 21.1 1.0 CB A:CYS134 4.3 18.9 1.0 ND1 A:HIS152 4.5 22.3 1.0 CB A:ALA154 4.5 18.6 1.0 CA A:CYS149 4.5 19.2 1.0 N A:HIS152 4.6 21.7 1.0 CA A:CYS129 4.6 15.3 1.0 N A:LEU132 4.7 19.4 1.0 CG A:HIS131 4.7 19.6 1.0 O A:CYS149 4.7 20.6 1.0 N A:CYS134 4.8 18.4 1.0 C A:CYS149 4.8 20.3 1.0 N A:CYS151 4.9 22.5 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:19.9 occ:1.00 FE2 A:FES200 0.0 19.9 1.0 ND1 A:HIS131 2.1 21.1 1.0 ND1 A:HIS152 2.1 22.3 1.0 S1 A:FES200 2.2 20.1 1.0 S2 A:FES200 2.2 18.6 1.0 FE1 A:FES200 2.7 18.2 1.0 CE1 A:HIS131 3.0 21.7 1.0 CE1 A:HIS152 3.1 23.1 1.0 CG A:HIS131 3.1 19.6 1.0 CG A:HIS152 3.1 22.0 1.0 CB A:HIS131 3.4 18.8 1.0 CB A:HIS152 3.4 21.9 1.0 N A:HIS152 3.8 21.7 1.0 CB A:CYS151 4.1 22.8 1.0 N A:LEU132 4.1 19.4 1.0 NE2 A:HIS131 4.1 22.1 1.0 CA A:HIS152 4.2 21.8 1.0 NE2 A:HIS152 4.2 23.8 1.0 CD2 A:HIS131 4.2 21.8 1.0 CD2 A:HIS152 4.2 23.6 1.0 SG A:CYS129 4.4 16.2 1.0 C A:CYS151 4.4 22.2 1.0 CB A:LEU132 4.5 20.1 1.0 SG A:CYS149 4.6 19.2 1.0 CG A:PRO166 4.6 23.2 1.0 CA A:HIS131 4.7 18.8 1.0 C A:HIS131 4.8 19.1 1.0 CA A:CYS151 4.8 22.7 1.0 CG A:LEU132 4.8 21.4 1.0 CA A:LEU132 4.8 19.6 1.0 C A:HIS152 4.9 21.5 1.0 CD1 A:LEU132 4.9 23.2 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