Iron in PDB 4b8n: Cytochrome B5 of Ostreococcus Tauri Virus 2

The structure of Cytochrome B5 of Ostreococcus Tauri Virus 2, PDB code: 4b8n was solved by M.Isupov, E.L.Reid, K.D.Weynberg, J.Love, W.H.Wilson, S.L.Kelly, D.C.Lamb, M.J.Allen, J.A.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.54 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.690, 58.500, 127.070, 90.00, 90.00, 90.00
R / Rfree (%)	18.768 / 25.368

The binding sites of Iron atom in the Cytochrome B5 of Ostreococcus Tauri Virus 2 (pdb code 4b8n). 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 B5 of Ostreococcus Tauri Virus 2, PDB code: 4b8n:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cytochrome B5 of Ostreococcus Tauri Virus 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome B5 of Ostreococcus Tauri Virus 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:22.1 occ:1.00 FE A:HEM201 0.0 22.1 1.0 NE2 A:HIS48 1.9 19.3 1.0 NA A:HEM201 2.0 23.2 1.0 NC A:HEM201 2.0 22.5 1.0 NE2 A:HIS71 2.0 18.1 1.0 NB A:HEM201 2.1 20.2 1.0 ND A:HEM201 2.1 22.7 1.0 CE1 A:HIS48 2.9 20.7 1.0 CD2 A:HIS48 3.0 22.7 1.0 C4C A:HEM201 3.0 24.4 1.0 CE1 A:HIS71 3.0 19.5 1.0 C4A A:HEM201 3.0 23.1 1.0 CD2 A:HIS71 3.1 21.5 1.0 C1C A:HEM201 3.1 22.1 1.0 C4B A:HEM201 3.1 20.9 1.0 C1D A:HEM201 3.1 22.6 1.0 C1A A:HEM201 3.1 22.0 1.0 C1B A:HEM201 3.1 22.0 1.0 C4D A:HEM201 3.2 24.9 1.0 CHD A:HEM201 3.4 19.4 1.0 CHC A:HEM201 3.4 20.1 1.0 CHB A:HEM201 3.5 20.8 1.0 CHA A:HEM201 3.5 23.9 1.0 ND1 A:HIS48 4.0 20.6 1.0 CG A:HIS48 4.1 20.4 1.0 ND1 A:HIS71 4.2 20.1 1.0 CG A:HIS71 4.2 22.4 1.0 C3C A:HEM201 4.3 21.9 1.0 C3A A:HEM201 4.3 21.9 1.0 C2A A:HEM201 4.3 22.7 1.0 C2C A:HEM201 4.4 22.8 1.0 C3B A:HEM201 4.4 23.9 1.0 C2D A:HEM201 4.4 29.7 1.0 C2B A:HEM201 4.4 23.1 1.0 C3D A:HEM201 4.5 27.1 1.0 N A:GLY50 4.8 20.5 1.0 CA A:GLY50 4.9 23.0 1.0

Iron binding site 2 out of 4 in the Cytochrome B5 of Ostreococcus Tauri Virus 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome B5 of Ostreococcus Tauri Virus 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:23.2 occ:1.00 FE B:HEM201 0.0 23.2 1.0 NE2 B:HIS48 1.9 19.1 1.0 NC B:HEM201 2.0 23.5 1.0 NA B:HEM201 2.0 27.1 1.0 NB B:HEM201 2.1 22.5 1.0 ND B:HEM201 2.1 28.5 1.0 NE2 B:HIS71 2.2 24.9 1.0 CE1 B:HIS48 2.8 25.0 1.0 CD2 B:HIS48 2.9 20.1 1.0 C4C B:HEM201 3.0 21.9 1.0 C4A B:HEM201 3.1 30.0 1.0 C1C B:HEM201 3.1 21.2 1.0 C1D B:HEM201 3.1 26.2 1.0 C4B B:HEM201 3.1 23.4 1.0 C1A B:HEM201 3.1 29.3 1.0 CD2 B:HIS71 3.1 19.6 1.0 C1B B:HEM201 3.1 22.4 1.0 CE1 B:HIS71 3.2 19.0 1.0 C4D B:HEM201 3.2 28.2 1.0 CHD B:HEM201 3.4 21.9 1.0 CHB B:HEM201 3.4 20.0 1.0 CHC B:HEM201 3.5 20.7 1.0 CHA B:HEM201 3.6 26.8 1.0 ND1 B:HIS48 4.0 24.4 1.0 CG B:HIS48 4.0 22.3 1.0 C3C B:HEM201 4.3 27.0 1.0 ND1 B:HIS71 4.3 21.9 1.0 CG B:HIS71 4.3 22.4 1.0 C3A B:HEM201 4.3 31.4 1.0 C2C B:HEM201 4.4 23.1 1.0 C2A B:HEM201 4.4 31.8 1.0 C3B B:HEM201 4.4 21.2 1.0 C2D B:HEM201 4.4 29.4 1.0 C2B B:HEM201 4.5 20.7 1.0 C3D B:HEM201 4.5 30.4 1.0 N B:GLY50 4.8 28.3 1.0 CA B:GLY50 4.9 27.8 1.0

Iron binding site 3 out of 4 in the Cytochrome B5 of Ostreococcus Tauri Virus 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome B5 of Ostreococcus Tauri Virus 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:34.5 occ:1.00 FE C:HEM201 0.0 34.5 1.0 NE2 C:HIS48 1.7 25.8 1.0 NC C:HEM201 2.0 38.9 1.0 NA C:HEM201 2.0 49.4 1.0 NE2 C:HIS71 2.1 29.7 1.0 NB C:HEM201 2.1 35.5 1.0 ND C:HEM201 2.2 38.4 1.0 CE1 C:HIS48 2.6 30.1 1.0 CD2 C:HIS48 2.8 26.6 1.0 C1C C:HEM201 3.0 33.0 1.0 CE1 C:HIS71 3.0 38.2 1.0 C4C C:HEM201 3.0 32.7 1.0 C4A C:HEM201 3.0 47.4 1.0 C1A C:HEM201 3.0 45.8 1.0 C4B C:HEM201 3.1 35.1 1.0 C1D C:HEM201 3.2 40.8 1.0 CD2 C:HIS71 3.2 36.4 1.0 C1B C:HEM201 3.2 43.7 1.0 C4D C:HEM201 3.2 41.4 1.0 CHC C:HEM201 3.4 30.3 1.0 CHD C:HEM201 3.5 32.5 1.0 CHB C:HEM201 3.5 41.1 1.0 CHA C:HEM201 3.5 40.3 1.0 ND1 C:HIS48 3.8 28.8 1.0 CG C:HIS48 3.9 24.7 1.0 ND1 C:HIS71 4.2 28.0 1.0 C3C C:HEM201 4.2 29.5 1.0 C3A C:HEM201 4.3 53.5 1.0 C2C C:HEM201 4.3 29.3 1.0 C2A C:HEM201 4.3 58.1 1.0 CG C:HIS71 4.3 32.5 1.0 C3B C:HEM201 4.4 34.6 1.0 C2D C:HEM201 4.5 36.3 1.0 C2B C:HEM201 4.5 39.0 1.0 C3D C:HEM201 4.6 45.5 1.0 N C:GLY50 4.8 33.5 1.0 CA C:GLY50 5.0 28.4 1.0

Iron binding site 4 out of 4 in the Cytochrome B5 of Ostreococcus Tauri Virus 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome B5 of Ostreococcus Tauri Virus 2 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:29.6 occ:1.00 FE D:HEM201 0.0 29.6 1.0 NE2 D:HIS48 1.9 21.9 1.0 NC D:HEM201 2.0 32.2 1.0 NA D:HEM201 2.0 34.5 1.0 NE2 D:HIS71 2.1 26.4 1.0 ND D:HEM201 2.1 38.8 1.0 NB D:HEM201 2.1 30.5 1.0 CD2 D:HIS48 2.8 24.9 1.0 CE1 D:HIS48 2.9 29.1 1.0 C4C D:HEM201 3.0 34.3 1.0 C1C D:HEM201 3.0 29.8 1.0 C4A D:HEM201 3.0 31.7 1.0 CD2 D:HIS71 3.1 24.6 1.0 C1A D:HEM201 3.1 31.7 1.0 CE1 D:HIS71 3.1 23.4 1.0 C4B D:HEM201 3.1 25.3 1.0 C1D D:HEM201 3.1 42.1 1.0 C4D D:HEM201 3.1 32.4 1.0 C1B D:HEM201 3.2 27.9 1.0 CHC D:HEM201 3.4 26.2 1.0 CHD D:HEM201 3.5 36.7 1.0 CHB D:HEM201 3.5 27.7 1.0 CHA D:HEM201 3.5 32.5 1.0 CG D:HIS48 4.0 27.0 1.0 ND1 D:HIS48 4.0 26.6 1.0 ND1 D:HIS71 4.3 24.6 1.0 CG D:HIS71 4.3 29.1 1.0 C3C D:HEM201 4.3 32.0 1.0 C3A D:HEM201 4.3 29.8 1.0 C2C D:HEM201 4.3 32.0 1.0 C2A D:HEM201 4.4 30.3 1.0 C3B D:HEM201 4.4 30.4 1.0 C3D D:HEM201 4.5 41.2 1.0 C2D D:HEM201 4.5 42.8 1.0 C2B D:HEM201 4.5 29.5 1.0 CA D:GLY50 4.8 35.0 1.0 N D:GLY50 4.8 36.0 1.0

E.L.Reid, K.D.Weynberg, J.Love, M.N.Isupov, J.A.Littlechild, W.H.Wilson, S.L.Kelly, D.C.Lamb, M.J.Allen. Functional and Structural Characterisation of A Viral Cytochrome B5. Febs Lett. V. 587 3633 2013.
ISSN: ISSN 0014-5793
PubMed: 24100138
DOI: 10.1016/J.FEBSLET.2013.09.035