Iron in PDB 4pwa: Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti

The structure of Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti, PDB code: 4pwa was solved by E.M.Laming, A.P.Mcgrath, M.J.Maher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.19 / 2.19
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	70.949, 129.327, 197.059, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 24.1

The binding sites of Iron atom in the Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti (pdb code 4pwa). 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 the C-Type Cytochrome Soru From Sinorhizobium Meliloti, PDB code: 4pwa:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti


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 the C-Type Cytochrome Soru From Sinorhizobium Meliloti within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:19.6 occ:1.00 FE A:HEC201 0.0 19.6 1.0 NB A:HEC201 2.0 19.9 1.0 NA A:HEC201 2.0 19.8 1.0 NE2 A:HIS51 2.0 22.5 1.0 NC A:HEC201 2.0 19.2 1.0 ND A:HEC201 2.1 19.4 1.0 SD A:MET87 2.4 24.2 1.0 CE1 A:HIS51 3.0 22.0 1.0 C1B A:HEC201 3.0 20.1 1.0 C4B A:HEC201 3.0 21.1 1.0 C4A A:HEC201 3.0 20.7 1.0 CD2 A:HIS51 3.0 21.4 1.0 C1A A:HEC201 3.0 20.4 1.0 C4C A:HEC201 3.0 20.7 1.0 C1D A:HEC201 3.1 19.8 1.0 C1C A:HEC201 3.1 20.7 1.0 C4D A:HEC201 3.1 19.8 1.0 CHB A:HEC201 3.4 20.2 1.0 CHD A:HEC201 3.4 20.9 1.0 CHC A:HEC201 3.4 21.1 1.0 CHA A:HEC201 3.4 20.0 1.0 CE A:MET87 3.4 21.6 1.0 CG A:MET87 3.5 24.6 1.0 ND1 A:HIS51 4.1 20.3 1.0 CG A:HIS51 4.1 21.4 1.0 C2B A:HEC201 4.2 20.2 1.0 C3B A:HEC201 4.2 20.6 1.0 C2A A:HEC201 4.2 21.4 1.0 C3A A:HEC201 4.2 20.2 1.0 C2C A:HEC201 4.3 18.9 1.0 C3C A:HEC201 4.3 19.9 1.0 CB A:MET87 4.3 25.6 1.0 C2D A:HEC201 4.3 17.5 1.0 C3D A:HEC201 4.3 18.8 1.0

Iron binding site 2 out of 4 in the Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti


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 the C-Type Cytochrome Soru From Sinorhizobium Meliloti within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:20.4 occ:1.00 FE B:HEC201 0.0 20.4 1.0 NA B:HEC201 2.0 19.7 1.0 NE2 B:HIS51 2.0 19.9 1.0 NC B:HEC201 2.0 17.0 1.0 NB B:HEC201 2.0 18.7 1.0 ND B:HEC201 2.1 18.5 1.0 SD B:MET87 2.4 20.6 1.0 CE1 B:HIS51 3.0 19.2 1.0 C1A B:HEC201 3.0 19.4 1.0 C1C B:HEC201 3.0 18.1 1.0 CD2 B:HIS51 3.0 18.5 1.0 C4B B:HEC201 3.0 18.2 1.0 C4A B:HEC201 3.0 19.4 1.0 C4D B:HEC201 3.0 18.0 1.0 C1D B:HEC201 3.1 18.8 1.0 C1B B:HEC201 3.1 19.7 1.0 C4C B:HEC201 3.1 19.2 1.0 CHC B:HEC201 3.4 17.5 1.0 CHA B:HEC201 3.4 20.1 1.0 CHD B:HEC201 3.4 19.2 1.0 CHB B:HEC201 3.4 20.4 1.0 CG B:MET87 3.4 19.9 1.0 CE B:MET87 3.5 17.0 1.0 ND1 B:HIS51 4.1 18.3 1.0 CG B:HIS51 4.1 19.5 1.0 CB B:MET87 4.2 21.4 1.0 C2A B:HEC201 4.2 19.4 1.0 C3A B:HEC201 4.2 19.2 1.0 C3B B:HEC201 4.3 20.4 1.0 C2C B:HEC201 4.3 17.1 1.0 C2B B:HEC201 4.3 21.0 1.0 C3D B:HEC201 4.3 18.6 1.0 C2D B:HEC201 4.3 18.0 1.0 C3C B:HEC201 4.3 16.1 1.0

Iron binding site 3 out of 4 in the Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti


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 the C-Type Cytochrome Soru From Sinorhizobium Meliloti within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:19.2 occ:1.00 FE C:HEC201 0.0 19.2 1.0 NE2 C:HIS51 1.9 17.1 1.0 NA C:HEC201 2.0 21.6 1.0 NC C:HEC201 2.0 21.1 1.0 NB C:HEC201 2.0 20.8 1.0 ND C:HEC201 2.1 21.9 1.0 SD C:MET87 2.3 18.8 1.0 CE1 C:HIS51 2.9 18.3 1.0 CD2 C:HIS51 2.9 17.6 1.0 C1C C:HEC201 3.0 21.2 1.0 C1A C:HEC201 3.0 22.3 1.0 C4B C:HEC201 3.0 20.4 1.0 C4A C:HEC201 3.1 19.7 1.0 C1B C:HEC201 3.1 19.9 1.0 C4C C:HEC201 3.1 21.5 1.0 C4D C:HEC201 3.1 20.9 1.0 C1D C:HEC201 3.1 22.3 1.0 CE C:MET87 3.3 19.4 1.0 CHC C:HEC201 3.4 21.6 1.0 CHA C:HEC201 3.4 22.1 1.0 CG C:MET87 3.4 20.2 1.0 CHB C:HEC201 3.4 20.3 1.0 CHD C:HEC201 3.5 22.8 1.0 ND1 C:HIS51 4.0 18.0 1.0 CG C:HIS51 4.1 18.6 1.0 C2A C:HEC201 4.2 19.9 1.0 CB C:MET87 4.2 21.3 1.0 C3A C:HEC201 4.3 19.1 1.0 C2C C:HEC201 4.3 18.9 1.0 C3B C:HEC201 4.3 21.3 1.0 C2B C:HEC201 4.3 20.5 1.0 C3C C:HEC201 4.3 18.8 1.0 C3D C:HEC201 4.3 21.4 1.0 C2D C:HEC201 4.3 21.3 1.0

Iron binding site 4 out of 4 in the Crystal Structure of the C-Type Cytochrome Soru From Sinorhizobium Meliloti


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 the C-Type Cytochrome Soru From Sinorhizobium Meliloti within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:21.0 occ:1.00 FE D:HEC201 0.0 21.0 1.0 NE2 D:HIS51 2.0 19.4 1.0 NB D:HEC201 2.0 21.8 1.0 NA D:HEC201 2.0 23.1 1.0 NC D:HEC201 2.1 22.3 1.0 ND D:HEC201 2.1 23.0 1.0 SD D:MET87 2.3 20.6 1.0 CE1 D:HIS51 3.0 18.8 1.0 CD2 D:HIS51 3.0 18.6 1.0 C1B D:HEC201 3.0 22.1 1.0 C1A D:HEC201 3.0 23.5 1.0 C4D D:HEC201 3.0 22.1 1.0 C4B D:HEC201 3.0 21.1 1.0 C1C D:HEC201 3.1 21.8 1.0 C4A D:HEC201 3.1 22.4 1.0 C4C D:HEC201 3.1 22.7 1.0 C1D D:HEC201 3.1 22.0 1.0 CHA D:HEC201 3.4 23.4 1.0 CE D:MET87 3.4 21.2 1.0 CHC D:HEC201 3.4 22.9 1.0 CHB D:HEC201 3.4 23.6 1.0 CHD D:HEC201 3.5 22.1 1.0 CG D:MET87 3.5 23.2 1.0 ND1 D:HIS51 4.1 17.8 1.0 CG D:HIS51 4.1 19.1 1.0 CB D:MET87 4.2 24.5 1.0 C2B D:HEC201 4.2 22.3 1.0 C3B D:HEC201 4.3 20.2 1.0 C2A D:HEC201 4.3 22.8 1.0 C2C D:HEC201 4.3 20.4 1.0 C3D D:HEC201 4.3 22.3 1.0 C3A D:HEC201 4.3 23.1 1.0 C3C D:HEC201 4.3 20.6 1.0 C2D D:HEC201 4.3 21.9 1.0

A.P.Mcgrath, E.L.Laming, G.P.Casas Garcia, M.Kvansakul, J.M.Guss, J.Trewhella, B.Calmes, P.V.Bernhardt, G.R.Hanson, U.Kappler, M.J.Maher. Structural Basis of Interprotein Electron Transfer in Bacterial Sulfite Oxidation. Elife V. 4 09066 2015.
ISSN: ESSN 2050-084X
PubMed: 26687009
DOI: 10.7554/ELIFE.09066