Iron in PDB 1i77: Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6

The structure of Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6, PDB code: 1i77 was solved by O.Einsle, S.Foerster, K.H.Mann, G.Fritz, A.Messerschmidt, P.M.H.Kroneck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.00 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.370, 49.390, 70.990, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 22.8

The binding sites of Iron atom in the Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6 (pdb code 1i77). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6, PDB code: 1i77:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe108 b:22.0 occ:1.00 FE A:HEM108 0.0 22.0 1.0 NE2 A:HIS34 1.9 13.2 1.0 ND A:HEM108 2.0 20.5 1.0 NC A:HEM108 2.0 17.2 1.0 NA A:HEM108 2.0 23.9 1.0 NB A:HEM108 2.0 20.6 1.0 NE2 A:HIS22 2.0 20.9 1.0 CE1 A:HIS34 2.9 15.4 1.0 CD2 A:HIS34 3.0 17.9 1.0 C1D A:HEM108 3.0 20.9 1.0 C1B A:HEM108 3.0 22.2 1.0 C4C A:HEM108 3.0 19.9 1.0 CE1 A:HIS22 3.0 21.7 1.0 C4A A:HEM108 3.0 24.3 1.0 C1A A:HEM108 3.0 23.8 1.0 C4D A:HEM108 3.0 21.4 1.0 C1C A:HEM108 3.1 20.0 1.0 C4B A:HEM108 3.1 21.8 1.0 CD2 A:HIS22 3.1 21.8 1.0 CHD A:HEM108 3.3 19.7 1.0 CHB A:HEM108 3.3 23.1 1.0 CHA A:HEM108 3.4 22.4 1.0 CHC A:HEM108 3.4 20.0 1.0 ND1 A:HIS34 4.0 17.0 1.0 CG A:HIS34 4.1 16.1 1.0 ND1 A:HIS22 4.2 22.7 1.0 CG A:HIS22 4.2 21.9 1.0 C2A A:HEM108 4.2 26.5 1.0 C3A A:HEM108 4.2 25.3 1.0 C2B A:HEM108 4.2 21.7 1.0 C2D A:HEM108 4.2 19.9 1.0 C3D A:HEM108 4.3 19.9 1.0 C3C A:HEM108 4.3 18.9 1.0 C2C A:HEM108 4.3 18.3 1.0 C3B A:HEM108 4.3 21.7 1.0 CE2 A:PHE20 4.7 20.9 1.0

Iron binding site 2 out of 4 in the Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe109 b:20.0 occ:1.00 FE A:HEM109 0.0 20.0 1.0 NE2 A:HIS35 1.9 18.4 1.0 NB A:HEM109 2.0 16.3 1.0 ND A:HEM109 2.0 20.1 1.0 NC A:HEM109 2.0 19.4 1.0 NE2 A:HIS52 2.0 13.8 1.0 NA A:HEM109 2.0 17.4 1.0 CE1 A:HIS35 2.8 19.7 1.0 CE1 A:HIS52 2.9 16.8 1.0 C1C A:HEM109 3.0 19.7 1.0 C1B A:HEM109 3.0 19.2 1.0 C4B A:HEM109 3.0 18.3 1.0 C1A A:HEM109 3.0 19.3 1.0 C4A A:HEM109 3.0 17.6 1.0 C4D A:HEM109 3.0 21.9 1.0 C4C A:HEM109 3.0 21.1 1.0 CD2 A:HIS52 3.0 16.1 1.0 C1D A:HEM109 3.0 21.9 1.0 CD2 A:HIS35 3.1 17.8 1.0 CHC A:HEM109 3.4 19.1 1.0 CHA A:HEM109 3.4 19.6 1.0 CHB A:HEM109 3.4 17.4 1.0 CHD A:HEM109 3.4 21.6 1.0 ND1 A:HIS35 4.0 18.4 1.0 ND1 A:HIS52 4.1 16.0 1.0 CG A:HIS35 4.2 20.4 1.0 CG A:HIS52 4.2 16.6 1.0 C2C A:HEM109 4.2 20.5 1.0 C2B A:HEM109 4.2 18.2 1.0 C2D A:HEM109 4.3 23.2 1.0 C3D A:HEM109 4.3 22.7 1.0 C3B A:HEM109 4.3 18.6 1.0 C2A A:HEM109 4.3 17.9 1.0 C3A A:HEM109 4.3 18.2 1.0 C3C A:HEM109 4.3 21.1 1.0

Iron binding site 3 out of 4 in the Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe110 b:20.1 occ:1.00 FE A:HEM110 0.0 20.1 1.0 ND A:HEM110 1.9 19.8 1.0 NA A:HEM110 2.0 19.5 1.0 NE2 A:HIS25 2.0 19.4 1.0 NB A:HEM110 2.0 17.1 1.0 NC A:HEM110 2.0 17.0 1.0 NE2 A:HIS83 2.0 19.4 1.0 C4D A:HEM110 3.0 20.8 1.0 CE1 A:HIS25 3.0 22.3 1.0 CE1 A:HIS83 3.0 18.2 1.0 C1D A:HEM110 3.0 20.8 1.0 C1A A:HEM110 3.0 21.5 1.0 CD2 A:HIS25 3.0 21.3 1.0 C4A A:HEM110 3.0 18.2 1.0 C1C A:HEM110 3.0 17.8 1.0 C4B A:HEM110 3.0 17.8 1.0 C4C A:HEM110 3.0 18.0 1.0 C1B A:HEM110 3.0 17.0 1.0 CD2 A:HIS83 3.1 18.5 1.0 CHA A:HEM110 3.4 20.2 1.0 CHD A:HEM110 3.4 19.8 1.0 CHC A:HEM110 3.4 16.1 1.0 CHB A:HEM110 3.4 16.9 1.0 ND1 A:HIS25 4.1 20.5 1.0 ND1 A:HIS83 4.1 17.2 1.0 CG A:HIS25 4.2 21.2 1.0 C3D A:HEM110 4.2 21.4 1.0 C2D A:HEM110 4.2 21.1 1.0 CG A:HIS83 4.2 17.6 1.0 C2A A:HEM110 4.2 21.9 1.0 C3A A:HEM110 4.3 19.4 1.0 C2C A:HEM110 4.3 15.3 1.0 C2B A:HEM110 4.3 16.4 1.0 C3C A:HEM110 4.3 17.5 1.0 C3B A:HEM110 4.3 16.9 1.0

Iron binding site 4 out of 4 in the Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe111 b:19.7 occ:1.00 FE A:HEM111 0.0 19.7 1.0 NA A:HEM111 2.0 18.0 1.0 NE2 A:HIS69 2.0 13.4 1.0 NC A:HEM111 2.0 16.4 1.0 ND A:HEM111 2.0 17.6 1.0 NB A:HEM111 2.0 18.8 1.0 NE2 A:HIS106 2.0 24.7 1.0 CE1 A:HIS106 3.0 23.8 1.0 CD2 A:HIS69 3.0 12.7 1.0 C4A A:HEM111 3.0 19.8 1.0 CE1 A:HIS69 3.0 13.1 1.0 C1A A:HEM111 3.0 19.6 1.0 C1D A:HEM111 3.0 18.9 1.0 C1B A:HEM111 3.0 19.8 1.0 C1C A:HEM111 3.0 19.5 1.0 C4C A:HEM111 3.0 19.1 1.0 C4B A:HEM111 3.0 20.1 1.0 C4D A:HEM111 3.1 19.1 1.0 CD2 A:HIS106 3.1 24.6 1.0 CHB A:HEM111 3.4 19.8 1.0 CHC A:HEM111 3.4 16.8 1.0 CHD A:HEM111 3.4 18.8 1.0 CHA A:HEM111 3.4 19.4 1.0 ND1 A:HIS69 4.1 15.2 1.0 CG A:HIS69 4.2 14.8 1.0 ND1 A:HIS106 4.2 23.1 1.0 C2D A:HEM111 4.2 17.5 1.0 CG A:HIS106 4.3 23.1 1.0 C2C A:HEM111 4.3 18.3 1.0 C2B A:HEM111 4.3 20.2 1.0 C2A A:HEM111 4.3 19.3 1.0 C3C A:HEM111 4.3 19.1 1.0 C3A A:HEM111 4.3 19.8 1.0 C3B A:HEM111 4.3 20.5 1.0 C3D A:HEM111 4.3 17.7 1.0

O.Einsle, S.Foerster, K.Mann, G.Fritz, A.Messerschmidt, P.M.Kroneck. Spectroscopic Investigation and Determination of Reactivity and Structure of the Tetraheme Cytochrome C3 From Desulfovibrio Desulfuricans Essex 6. Eur.J.Biochem. V. 268 3028 2001.
ISSN: ISSN 0014-2956
PubMed: 11358521
DOI: 10.1046/J.1432-1327.2001.02195.X