Iron in PDB 3o1y: Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface

The structure of Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface, PDB code: 3o1y was solved by M.De March, R.De Zorzi, N.Demitri, C.Gabbiani, A.Guerri, A.Casini, L.Messori, S.Geremia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.01 / 1.75
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.695, 79.695, 89.247, 90.00, 90.00, 120.00
R / Rfree (%)	18.6 / 24.8

The binding sites of Iron atom in the Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface (pdb code 3o1y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface, PDB code: 3o1y:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe105 b:12.2 occ:1.00 FE A:HEC105 0.0 12.2 1.0 NE2 A:HIS18 2.0 10.3 1.0 ND A:HEC105 2.0 8.1 1.0 NA A:HEC105 2.0 9.2 1.0 NC A:HEC105 2.1 10.2 1.0 NB A:HEC105 2.1 7.3 1.0 SD A:MET80 2.3 11.9 1.0 CE1 A:HIS18 2.9 10.2 1.0 C1D A:HEC105 3.0 9.1 1.0 C4D A:HEC105 3.0 11.2 1.0 C1A A:HEC105 3.1 10.1 1.0 C4C A:HEC105 3.1 9.0 1.0 C4B A:HEC105 3.1 10.1 1.0 C1B A:HEC105 3.1 9.9 1.0 CD2 A:HIS18 3.1 10.5 1.0 C1C A:HEC105 3.1 9.8 1.0 C4A A:HEC105 3.1 11.7 1.0 CHA A:HEC105 3.4 9.5 1.0 CHD A:HEC105 3.4 8.6 1.0 CG A:MET80 3.4 8.5 1.0 CE A:MET80 3.4 10.0 1.0 CHC A:HEC105 3.5 10.0 1.0 CHB A:HEC105 3.5 8.6 1.0 ND1 A:HIS18 4.1 11.8 1.0 CG A:HIS18 4.2 9.2 1.0 C2D A:HEC105 4.2 10.3 1.0 C3B A:HEC105 4.3 8.6 1.0 C3D A:HEC105 4.3 9.5 1.0 C2B A:HEC105 4.3 9.0 1.0 C3C A:HEC105 4.3 9.3 1.0 CB A:MET80 4.3 10.1 1.0 C2C A:HEC105 4.3 8.4 1.0 C2A A:HEC105 4.3 11.1 1.0 C3A A:HEC105 4.3 11.2 1.0 OH A:TYR67 4.5 11.7 1.0

Iron binding site 2 out of 3 in the Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe105 b:12.3 occ:1.00 FE B:HEC105 0.0 12.3 1.0 NE2 B:HIS18 2.0 11.2 1.0 NB B:HEC105 2.0 9.7 1.0 NC B:HEC105 2.1 10.8 1.0 NA B:HEC105 2.1 8.6 1.0 ND B:HEC105 2.1 10.9 1.0 SD B:MET80 2.4 11.0 1.0 CE1 B:HIS18 2.9 9.2 1.0 C1B B:HEC105 3.0 12.0 1.0 CD2 B:HIS18 3.0 9.8 1.0 C4B B:HEC105 3.0 14.2 1.0 C4A B:HEC105 3.0 13.8 1.0 C4C B:HEC105 3.0 11.5 1.0 C1D B:HEC105 3.1 12.4 1.0 C1A B:HEC105 3.1 11.3 1.0 C4D B:HEC105 3.1 12.8 1.0 C1C B:HEC105 3.1 12.8 1.0 CHB B:HEC105 3.4 10.6 1.0 CHD B:HEC105 3.4 10.2 1.0 CE B:MET80 3.4 9.9 1.0 CHA B:HEC105 3.4 10.0 1.0 CHC B:HEC105 3.5 11.1 1.0 CG B:MET80 3.5 8.8 1.0 ND1 B:HIS18 4.0 11.6 1.0 CG B:HIS18 4.1 9.6 1.0 C2B B:HEC105 4.2 11.0 1.0 C3B B:HEC105 4.2 11.0 1.0 C3A B:HEC105 4.3 7.9 1.0 C3C B:HEC105 4.3 9.6 1.0 CB B:MET80 4.3 9.9 1.0 C2D B:HEC105 4.3 11.6 1.0 C2A B:HEC105 4.3 11.0 1.0 C3D B:HEC105 4.3 9.3 1.0 C2C B:HEC105 4.3 9.5 1.0 OH B:TYR67 4.5 13.1 1.0

Iron binding site 3 out of 3 in the Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Electron Transfer Complexes: Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe105 b:11.1 occ:1.00 FE C:HEC105 0.0 11.1 1.0 NE2 C:HIS18 2.0 11.2 1.0 NB C:HEC105 2.0 8.9 1.0 NC C:HEC105 2.1 9.0 1.0 ND C:HEC105 2.1 10.1 1.0 NA C:HEC105 2.1 10.7 1.0 SD C:MET80 2.3 10.8 1.0 CE1 C:HIS18 2.9 8.5 1.0 C1B C:HEC105 3.0 7.8 1.0 C4B C:HEC105 3.0 8.4 1.0 CD2 C:HIS18 3.0 9.5 1.0 C4A C:HEC105 3.0 11.6 1.0 C1D C:HEC105 3.0 11.1 1.0 C1C C:HEC105 3.1 11.0 1.0 C4C C:HEC105 3.1 9.1 1.0 C1A C:HEC105 3.1 9.5 1.0 C4D C:HEC105 3.1 10.9 1.0 CHB C:HEC105 3.4 10.3 1.0 CE C:MET80 3.4 10.7 1.0 CHC C:HEC105 3.4 10.7 1.0 CHD C:HEC105 3.4 8.1 1.0 CG C:MET80 3.5 9.9 1.0 CHA C:HEC105 3.5 9.7 1.0 ND1 C:HIS18 4.0 11.4 1.0 CG C:HIS18 4.1 9.7 1.0 C3B C:HEC105 4.2 10.6 1.0 C2B C:HEC105 4.2 10.8 1.0 C3A C:HEC105 4.3 8.7 1.0 C2D C:HEC105 4.3 9.3 1.0 C3C C:HEC105 4.3 8.9 1.0 C2C C:HEC105 4.3 8.6 1.0 C2A C:HEC105 4.3 10.0 1.0 CB C:MET80 4.3 10.0 1.0 C3D C:HEC105 4.3 11.1 1.0 OH C:TYR67 4.5 11.5 1.0

M.De March, N.Demitri, R.De Zorzi, A.Casini, C.Gabbiani, A.Guerri, L.Messori, S.Geremia. Nitrate As A Probe of Cytochrome C Surface: Crystallographic Identification of Crucial "Hot Spots" For Protein-Protein Recognition. J. Inorg. Biochem. V. 135 58 2014.
ISSN: ISSN 1873-3344
PubMed: 24662464
DOI: 10.1016/J.JINORGBIO.2014.02.015