Iron in PDB 3iq6: Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces

The structure of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces, PDB code: 3iq6 was solved by J.N.Brodin, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.265, 76.770, 177.566, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 29.6

The structure of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Iron atom in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces (pdb code 3iq6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces, PDB code: 3iq6:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:52.8 occ:1.00 FE A:HEM150 0.0 52.8 1.0 ND A:HEM150 1.8 60.4 1.0 NB A:HEM150 2.0 51.5 1.0 NC A:HEM150 2.0 55.1 1.0 NA A:HEM150 2.1 61.1 1.0 NE2 A:HIS102 2.1 49.9 1.0 SD A:MET7 2.1 49.1 1.0 C4D A:HEM150 2.9 62.0 1.0 C1D A:HEM150 2.9 61.4 1.0 CD2 A:HIS102 3.0 54.4 1.0 C4B A:HEM150 3.1 51.3 1.0 C4C A:HEM150 3.1 54.0 1.0 C1A A:HEM150 3.1 63.8 1.0 C1C A:HEM150 3.1 51.0 1.0 C1B A:HEM150 3.1 53.9 1.0 CE1 A:HIS102 3.1 54.4 1.0 C4A A:HEM150 3.2 60.7 1.0 CHD A:HEM150 3.3 59.5 1.0 CHA A:HEM150 3.3 64.1 1.0 CHC A:HEM150 3.4 53.5 1.0 CE A:MET7 3.5 50.4 1.0 CHB A:HEM150 3.5 57.7 1.0 CG A:MET7 3.6 54.3 1.0 C2D A:HEM150 4.1 61.9 1.0 C3D A:HEM150 4.1 62.7 1.0 CG A:HIS102 4.2 53.9 1.0 ND1 A:HIS102 4.2 50.3 1.0 C2C A:HEM150 4.3 50.6 1.0 C3C A:HEM150 4.3 51.7 1.0 C3B A:HEM150 4.3 51.7 1.0 C2B A:HEM150 4.3 51.8 1.0 C2A A:HEM150 4.4 68.0 1.0 CB A:MET7 4.4 50.4 1.0 C3A A:HEM150 4.4 66.3 1.0

Iron binding site 2 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:29.2 occ:1.00 FE B:HEM150 0.0 29.2 1.0 NB B:HEM150 1.9 29.6 1.0 ND B:HEM150 2.0 31.7 1.0 NC B:HEM150 2.0 30.5 1.0 NE2 B:HIS102 2.0 29.2 1.0 NA B:HEM150 2.0 31.9 1.0 SD B:MET7 2.3 35.4 1.0 C4B B:HEM150 2.9 30.8 1.0 C1C B:HEM150 2.9 29.1 1.0 C4D B:HEM150 2.9 33.9 1.0 C1A B:HEM150 3.0 34.3 1.0 CE1 B:HIS102 3.0 25.0 1.0 CD2 B:HIS102 3.0 25.3 1.0 C1D B:HEM150 3.1 31.1 1.0 C1B B:HEM150 3.1 31.6 1.0 C4C B:HEM150 3.1 29.7 1.0 C4A B:HEM150 3.2 30.6 1.0 CHC B:HEM150 3.2 30.0 1.0 CHA B:HEM150 3.3 30.4 1.0 CG B:MET7 3.4 33.0 1.0 CE B:MET7 3.4 37.6 1.0 CHD B:HEM150 3.5 28.7 1.0 CHB B:HEM150 3.6 33.1 1.0 ND1 B:HIS102 4.1 29.8 1.0 CG B:HIS102 4.1 29.2 1.0 C3B B:HEM150 4.2 29.8 1.0 CB B:MET7 4.2 35.3 1.0 C2C B:HEM150 4.2 25.3 1.0 C3D B:HEM150 4.2 32.0 1.0 C2A B:HEM150 4.3 39.8 1.0 C2D B:HEM150 4.3 33.6 1.0 C2B B:HEM150 4.3 29.2 1.0 C3C B:HEM150 4.3 31.3 1.0 C3A B:HEM150 4.4 32.5 1.0

Iron binding site 3 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe150 b:28.5 occ:1.00 FE C:HEM150 0.0 28.5 1.0 NC C:HEM150 1.9 19.8 1.0 NE2 C:HIS102 2.0 32.1 1.0 NA C:HEM150 2.0 30.7 1.0 ND C:HEM150 2.0 30.8 1.0 NB C:HEM150 2.0 23.7 1.0 SD C:MET7 2.2 35.9 1.0 CE1 C:HIS102 2.8 30.5 1.0 C1C C:HEM150 3.0 18.3 1.0 C4C C:HEM150 3.0 22.5 1.0 C1A C:HEM150 3.0 31.8 1.0 C1D C:HEM150 3.0 32.0 1.0 C4D C:HEM150 3.0 32.8 1.0 C4B C:HEM150 3.1 19.9 1.0 C4A C:HEM150 3.1 30.0 1.0 CD2 C:HIS102 3.1 29.9 1.0 C1B C:HEM150 3.1 22.3 1.0 CHD C:HEM150 3.4 26.3 1.0 CHC C:HEM150 3.4 16.2 1.0 CHA C:HEM150 3.4 32.0 1.0 CE C:MET7 3.4 32.7 1.0 CHB C:HEM150 3.4 27.3 1.0 CG C:MET7 3.6 35.6 1.0 ND1 C:HIS102 4.0 29.3 1.0 CG C:HIS102 4.1 25.5 1.0 C2C C:HEM150 4.2 19.7 1.0 C3C C:HEM150 4.3 22.7 1.0 C2A C:HEM150 4.3 32.8 1.0 C2D C:HEM150 4.3 33.8 1.0 C3D C:HEM150 4.3 38.1 1.0 C2B C:HEM150 4.3 19.9 1.0 C3B C:HEM150 4.3 17.2 1.0 C3A C:HEM150 4.3 33.6 1.0 NH1 C:ARG106 4.3 59.4 1.0 CB C:MET7 4.4 35.9 1.0

Iron binding site 4 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


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 A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe150 b:35.8 occ:1.00 FE D:HEM150 0.0 35.8 1.0 NB D:HEM150 1.9 38.1 1.0 NE2 D:HIS102 1.9 41.0 1.0 ND D:HEM150 2.0 35.6 1.0 NC D:HEM150 2.0 34.6 1.0 NA D:HEM150 2.1 41.1 1.0 SD D:MET7 2.4 36.1 1.0 CE1 D:HIS102 2.7 37.4 1.0 C4B D:HEM150 2.9 38.9 1.0 C1B D:HEM150 2.9 42.1 1.0 C1C D:HEM150 3.0 32.2 1.0 C1D D:HEM150 3.0 39.0 1.0 C4D D:HEM150 3.0 42.0 1.0 CD2 D:HIS102 3.0 35.9 1.0 C4C D:HEM150 3.1 35.0 1.0 C4A D:HEM150 3.1 41.0 1.0 C1A D:HEM150 3.2 42.8 1.0 CHC D:HEM150 3.3 36.5 1.0 CHB D:HEM150 3.4 43.0 1.0 CHD D:HEM150 3.4 36.6 1.0 CHA D:HEM150 3.5 42.1 1.0 CG D:MET7 3.5 36.0 1.0 CE D:MET7 3.5 37.8 1.0 ND1 D:HIS102 3.9 34.7 1.0 CG D:HIS102 4.1 39.1 1.0 C2B D:HEM150 4.2 42.6 1.0 C3B D:HEM150 4.2 40.9 1.0 C2C D:HEM150 4.2 33.0 1.0 C2D D:HEM150 4.3 38.5 1.0 C3D D:HEM150 4.3 40.2 1.0 C3C D:HEM150 4.3 34.5 1.0 CB D:MET7 4.3 36.6 1.0 C3A D:HEM150 4.4 44.7 1.0 C2A D:HEM150 4.5 45.7 1.0

Iron binding site 5 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe150 b:24.6 occ:1.00 FE E:HEM150 0.0 24.6 1.0 ND E:HEM150 1.8 25.4 1.0 NC E:HEM150 1.9 22.2 1.0 NA E:HEM150 1.9 15.2 1.0 NE2 E:HIS102 2.1 37.4 1.0 NB E:HEM150 2.1 17.7 1.0 SD E:MET7 2.3 28.6 1.0 C4D E:HEM150 2.8 28.0 1.0 C1A E:HEM150 2.8 19.5 1.0 C1C E:HEM150 2.9 23.0 1.0 C1D E:HEM150 3.0 23.7 1.0 C4C E:HEM150 3.0 26.0 1.0 CE1 E:HIS102 3.0 29.6 1.0 C4B E:HEM150 3.1 22.2 1.0 C4A E:HEM150 3.1 19.8 1.0 CD2 E:HIS102 3.1 33.2 1.0 CHA E:HEM150 3.2 21.0 1.0 C1B E:HEM150 3.2 20.0 1.0 CE E:MET7 3.3 25.6 1.0 CHC E:HEM150 3.3 21.0 1.0 CHD E:HEM150 3.4 23.8 1.0 CG E:MET7 3.4 25.6 1.0 CHB E:HEM150 3.6 22.3 1.0 C3D E:HEM150 4.0 28.0 1.0 C2D E:HEM150 4.1 26.3 1.0 C2A E:HEM150 4.2 21.8 1.0 ND1 E:HIS102 4.2 37.4 1.0 C3C E:HEM150 4.2 27.6 1.0 C2C E:HEM150 4.2 22.8 1.0 CG E:HIS102 4.2 38.5 1.0 CB E:MET7 4.2 29.3 1.0 C3A E:HEM150 4.3 24.1 1.0 C3B E:HEM150 4.4 21.9 1.0 C2B E:HEM150 4.4 23.7 1.0 NH1 E:ARG106 4.6 38.1 1.0

Iron binding site 6 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe150 b:32.6 occ:1.00 FE F:HEM150 0.0 32.6 1.0 ND F:HEM150 1.8 35.8 1.0 NC F:HEM150 1.9 31.0 1.0 NE2 F:HIS102 2.0 21.2 1.0 NA F:HEM150 2.1 40.1 1.0 NB F:HEM150 2.1 30.9 1.0 SD F:MET7 2.3 37.9 1.0 C1D F:HEM150 2.8 36.3 1.0 C4D F:HEM150 2.9 38.5 1.0 C4C F:HEM150 2.9 32.1 1.0 C1C F:HEM150 3.0 30.5 1.0 CE1 F:HIS102 3.0 19.3 1.0 CD2 F:HIS102 3.1 22.0 1.0 C1A F:HEM150 3.1 39.4 1.0 C4B F:HEM150 3.1 30.5 1.0 C4A F:HEM150 3.1 39.9 1.0 C1B F:HEM150 3.2 30.3 1.0 CHD F:HEM150 3.2 30.1 1.0 CE F:MET7 3.3 37.6 1.0 CG F:MET7 3.4 42.0 1.0 CHA F:HEM150 3.4 40.2 1.0 CHC F:HEM150 3.4 28.4 1.0 CHB F:HEM150 3.5 36.0 1.0 C2D F:HEM150 4.1 35.9 1.0 ND1 F:HIS102 4.1 23.1 1.0 C3D F:HEM150 4.2 38.0 1.0 CG F:HIS102 4.2 23.7 1.0 CB F:MET7 4.2 45.3 1.0 C2C F:HEM150 4.2 29.4 1.0 C3C F:HEM150 4.2 29.7 1.0 C3A F:HEM150 4.4 40.0 1.0 C3B F:HEM150 4.4 30.4 1.0 C2A F:HEM150 4.4 44.9 1.0 C2B F:HEM150 4.4 31.4 1.0 NH1 F:ARG106 4.7 54.6 1.0

Iron binding site 7 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe150 b:53.4 occ:1.00 FE G:HEM150 0.0 53.4 1.0 NB G:HEM150 1.9 53.0 1.0 NE2 G:HIS102 2.0 45.5 1.0 NC G:HEM150 2.0 56.4 1.0 NA G:HEM150 2.0 58.9 1.0 ND G:HEM150 2.0 61.4 1.0 SD G:MET7 2.2 52.8 1.0 C4B G:HEM150 2.9 51.4 1.0 C1C G:HEM150 2.9 53.7 1.0 CE1 G:HIS102 2.9 49.1 1.0 C1A G:HEM150 3.0 60.2 1.0 CD2 G:HIS102 3.0 49.8 1.0 C4D G:HEM150 3.0 63.5 1.0 C1B G:HEM150 3.0 52.1 1.0 C4A G:HEM150 3.1 57.7 1.0 C4C G:HEM150 3.1 57.0 1.0 C1D G:HEM150 3.2 62.1 1.0 CHC G:HEM150 3.2 51.3 1.0 CHA G:HEM150 3.3 61.1 1.0 CHB G:HEM150 3.4 53.5 1.0 CE G:MET7 3.4 50.0 1.0 CHD G:HEM150 3.5 60.6 1.0 CG G:MET7 3.6 50.2 1.0 ND1 G:HIS102 4.1 48.7 1.0 CG G:HIS102 4.1 50.5 1.0 C3B G:HEM150 4.2 50.0 1.0 C2C G:HEM150 4.2 53.9 1.0 C2B G:HEM150 4.2 52.7 1.0 C2A G:HEM150 4.3 63.8 1.0 C3A G:HEM150 4.3 60.7 1.0 C3C G:HEM150 4.3 56.0 1.0 C3D G:HEM150 4.3 65.2 1.0 CB G:MET7 4.4 52.8 1.0 C2D G:HEM150 4.4 63.0 1.0

Iron binding site 8 out of 8 in the Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of A Tetrameric Zn-Bound Cytochrome CB562 Complex with Covalently and Non-Covalently Stabilized Interfaces within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe150 b:35.8 occ:1.00 FE H:HEM150 0.0 35.8 1.0 ND H:HEM150 1.8 36.5 1.0 NA H:HEM150 1.9 40.4 1.0 NE2 H:HIS102 2.1 37.4 1.0 NB H:HEM150 2.1 32.5 1.0 NC H:HEM150 2.1 35.0 1.0 SD H:MET7 2.3 42.7 1.0 C4D H:HEM150 2.8 38.7 1.0 C1A H:HEM150 2.9 42.4 1.0 C1D H:HEM150 2.9 39.5 1.0 C4A H:HEM150 3.0 41.9 1.0 CE1 H:HIS102 3.0 41.4 1.0 CD2 H:HIS102 3.1 40.4 1.0 C1B H:HEM150 3.1 37.7 1.0 C4C H:HEM150 3.1 38.9 1.0 C4B H:HEM150 3.2 34.0 1.0 CHA H:HEM150 3.2 41.0 1.0 C1C H:HEM150 3.2 33.4 1.0 CHD H:HEM150 3.4 38.7 1.0 CHB H:HEM150 3.4 37.2 1.0 CG H:MET7 3.5 42.3 1.0 CHC H:HEM150 3.5 33.9 1.0 CE H:MET7 3.6 46.3 1.0 C3D H:HEM150 4.1 40.5 1.0 ND1 H:HIS102 4.1 39.2 1.0 C2D H:HEM150 4.1 41.7 1.0 C2A H:HEM150 4.2 46.5 1.0 C3A H:HEM150 4.2 42.6 1.0 CB H:MET7 4.2 41.1 1.0 CG H:HIS102 4.2 42.2 1.0 C2B H:HEM150 4.4 38.2 1.0 C3B H:HEM150 4.4 33.6 1.0 C3C H:HEM150 4.4 35.6 1.0 C2C H:HEM150 4.5 38.0 1.0

J.D.Brodin, A.Medina-Morales, T.Ni, E.N.Salgado, X.I.Ambroggio, F.A.Tezcan. Evolution of Metal Selectivity in Templated Protein Interfaces. J.Am.Chem.Soc. V. 132 8610 2010.
ISSN: ISSN 0002-7863
PubMed: 20515031
DOI: 10.1021/JA910844N