Iron in PDB 3o20: 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: 3o20 was solved by M.De March, R.De Zorzi, A.Casini, L.Messori, S.Geremia, N.Demitri, C.Gabbiani, A.Guerri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	65.09 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.092, 52.029, 77.749, 90.00, 123.07, 90.00
R / Rfree (%)	19.3 / 27.6

The binding sites of Iron atom in the Electron Transfer Complexes:Experimental Mapping of the Redox- Dependent Cytochrome C Electrostatic Surface (pdb code 3o20). 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: 3o20:
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:5.3 occ:1.00 FE A:HEC105 0.0 5.3 1.0 NB A:HEC105 2.0 3.1 1.0 ND A:HEC105 2.0 4.8 1.0 NE2 A:HIS18 2.0 7.6 1.0 NC A:HEC105 2.1 5.0 1.0 NA A:HEC105 2.2 5.4 1.0 SD A:MET80 2.4 4.8 1.0 C1D A:HEC105 3.0 9.4 1.0 C4C A:HEC105 3.0 5.2 1.0 C1B A:HEC105 3.0 7.1 1.0 CD2 A:HIS18 3.0 7.4 1.0 CE1 A:HIS18 3.0 8.6 1.0 C4B A:HEC105 3.1 4.0 1.0 C4D A:HEC105 3.1 5.9 1.0 C1C A:HEC105 3.1 5.7 1.0 C4A A:HEC105 3.2 6.8 1.0 C1A A:HEC105 3.2 6.8 1.0 CHD A:HEC105 3.3 2.4 1.0 CE A:MET80 3.4 2.2 1.0 CG A:MET80 3.4 4.0 1.0 CHB A:HEC105 3.4 3.7 1.0 CHA A:HEC105 3.5 3.6 1.0 CHC A:HEC105 3.5 2.0 1.0 ND1 A:HIS18 4.1 7.0 1.0 CG A:HIS18 4.2 7.2 1.0 CB A:MET80 4.2 4.8 1.0 C3B A:HEC105 4.2 2.0 1.0 C2D A:HEC105 4.2 3.5 1.0 C2B A:HEC105 4.2 4.9 1.0 C3D A:HEC105 4.3 5.1 1.0 C3C A:HEC105 4.3 2.5 1.0 C2C A:HEC105 4.3 2.4 1.0 C2A A:HEC105 4.4 5.2 1.0 C3A A:HEC105 4.4 6.7 1.0 OH A:TYR67 4.9 7.6 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:7.8 occ:1.00 FE B:HEC105 0.0 7.8 1.0 NB B:HEC105 2.0 4.8 1.0 NE2 B:HIS18 2.0 8.8 1.0 NC B:HEC105 2.0 6.5 1.0 NA B:HEC105 2.2 4.9 1.0 ND B:HEC105 2.2 5.5 1.0 SD B:MET80 2.4 4.7 1.0 CD2 B:HIS18 3.0 7.4 1.0 C1B B:HEC105 3.0 2.0 1.0 C4B B:HEC105 3.0 6.5 1.0 CE1 B:HIS18 3.0 9.1 1.0 C4C B:HEC105 3.0 3.5 1.0 C1C B:HEC105 3.0 6.3 1.0 C4A B:HEC105 3.1 3.2 1.0 C1D B:HEC105 3.1 3.7 1.0 C1A B:HEC105 3.2 3.1 1.0 C4D B:HEC105 3.2 4.1 1.0 CHB B:HEC105 3.4 5.0 1.0 CHD B:HEC105 3.4 3.0 1.0 CE B:MET80 3.4 2.0 1.0 CHC B:HEC105 3.4 4.0 1.0 CG B:MET80 3.5 4.2 1.0 CHA B:HEC105 3.5 3.7 1.0 ND1 B:HIS18 4.1 7.6 1.0 CG B:HIS18 4.1 7.3 1.0 C3B B:HEC105 4.2 4.9 1.0 C2B B:HEC105 4.2 5.5 1.0 CB B:MET80 4.2 5.0 1.0 C2C B:HEC105 4.2 3.2 1.0 C3C B:HEC105 4.2 6.0 1.0 C2A B:HEC105 4.4 7.6 1.0 C3D B:HEC105 4.4 3.2 1.0 C3A B:HEC105 4.4 5.2 1.0 C2D B:HEC105 4.4 3.2 1.0 OH B:TYR67 4.9 7.5 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:9.3 occ:1.00 FE C:HEC105 0.0 9.3 1.0 NB C:HEC105 2.0 6.5 1.0 NC C:HEC105 2.0 7.5 1.0 NE2 C:HIS18 2.0 8.5 1.0 ND C:HEC105 2.0 5.8 1.0 NA C:HEC105 2.2 7.0 1.0 SD C:MET80 2.3 7.0 1.0 CD2 C:HIS18 3.0 7.7 1.0 C4B C:HEC105 3.0 8.0 1.0 C1D C:HEC105 3.0 7.3 1.0 C4C C:HEC105 3.0 6.5 1.0 C1C C:HEC105 3.0 5.6 1.0 C1B C:HEC105 3.1 6.3 1.0 CE1 C:HIS18 3.1 8.7 1.0 C4D C:HEC105 3.1 10.1 1.0 C4A C:HEC105 3.1 5.5 1.0 C1A C:HEC105 3.2 8.0 1.0 CHD C:HEC105 3.3 7.1 1.0 CE C:MET80 3.3 3.2 1.0 CG C:MET80 3.3 4.1 1.0 CHC C:HEC105 3.4 8.2 1.0 CHB C:HEC105 3.5 6.7 1.0 CHA C:HEC105 3.5 5.6 1.0 CG C:HIS18 4.1 6.8 1.0 CB C:MET80 4.1 5.7 1.0 ND1 C:HIS18 4.1 7.5 1.0 C3B C:HEC105 4.2 5.0 1.0 C2B C:HEC105 4.2 7.0 1.0 C3C C:HEC105 4.3 5.3 1.0 C2D C:HEC105 4.3 9.9 1.0 C2C C:HEC105 4.3 6.0 1.0 C3D C:HEC105 4.3 8.9 1.0 C3A C:HEC105 4.4 3.9 1.0 C2A C:HEC105 4.4 3.7 1.0 OH C:TYR67 4.8 8.0 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