Iron in PDB 2qla: Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules

The structure of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules, PDB code: 2qla was solved by F.A.Tezcan, E.N.Salgado, J.Faraone-Mennella, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.984, 66.659, 68.901, 90.00, 90.00, 90.00
R / Rfree (%)	24.8 / 29.5

The structure of Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Iron atom in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules (pdb code 2qla). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules, PDB code: 2qla:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


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 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:29.2 occ:1.00 FE A:HEM150 0.0 29.2 1.0 NA A:HEM150 1.9 33.3 1.0 NB A:HEM150 1.9 31.5 1.0 ND A:HEM150 2.0 34.3 1.0 NE2 A:HIS102 2.1 36.7 1.0 NC A:HEM150 2.2 29.3 1.0 SD A:MET7 2.4 25.9 1.0 CE1 A:HIS102 2.9 38.6 1.0 C4A A:HEM150 2.9 33.1 1.0 C1B A:HEM150 2.9 30.9 1.0 C1A A:HEM150 3.0 34.0 1.0 C4D A:HEM150 3.0 36.1 1.0 C4B A:HEM150 3.1 29.7 1.0 C1D A:HEM150 3.1 35.1 1.0 C1C A:HEM150 3.2 26.6 1.0 C4C A:HEM150 3.2 30.0 1.0 CD2 A:HIS102 3.2 39.2 1.0 CHB A:HEM150 3.2 32.7 1.0 CHA A:HEM150 3.3 34.4 1.0 CHC A:HEM150 3.5 27.3 1.0 CHD A:HEM150 3.5 34.2 1.0 CG A:MET7 3.5 33.5 1.0 CE A:MET7 3.6 31.2 1.0 ND1 A:HIS102 4.1 39.8 1.0 C3A A:HEM150 4.1 34.8 1.0 CB A:MET7 4.2 36.1 1.0 C2B A:HEM150 4.2 28.8 1.0 C2A A:HEM150 4.2 37.3 1.0 CG A:HIS102 4.3 42.0 1.0 C3B A:HEM150 4.3 29.9 1.0 C3D A:HEM150 4.3 39.0 1.0 C2D A:HEM150 4.3 38.2 1.0 C2C A:HEM150 4.5 27.9 1.0 C3C A:HEM150 4.5 27.7 1.0 CA A:MET7 5.0 37.6 1.0

Iron binding site 2 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


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 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe151 b:25.7 occ:1.00 FE B:HEM151 0.0 25.7 1.0 ND B:HEM151 1.9 30.9 1.0 NA B:HEM151 1.9 29.7 1.0 NB B:HEM151 2.1 27.4 1.0 NE2 B:HIS102 2.1 37.8 1.0 NC B:HEM151 2.1 28.5 1.0 SD B:MET7 2.4 19.2 1.0 CE1 B:HIS102 2.9 41.1 1.0 C4D B:HEM151 2.9 33.5 1.0 C4A B:HEM151 3.0 29.4 1.0 C1A B:HEM151 3.0 30.8 1.0 C1D B:HEM151 3.0 31.9 1.0 C1B B:HEM151 3.0 27.7 1.0 C4B B:HEM151 3.1 26.9 1.0 C4C B:HEM151 3.2 26.7 1.0 C1C B:HEM151 3.2 28.1 1.0 CD2 B:HIS102 3.2 40.9 1.0 CHA B:HEM151 3.3 31.2 1.0 CHB B:HEM151 3.3 26.9 1.0 CHD B:HEM151 3.4 29.1 1.0 CHC B:HEM151 3.5 27.2 1.0 CG B:MET7 3.5 26.1 1.0 CE B:MET7 3.5 21.5 1.0 ND1 B:HIS102 4.0 42.8 1.0 C3D B:HEM151 4.2 38.1 1.0 C2D B:HEM151 4.2 35.5 1.0 C3A B:HEM151 4.2 30.8 1.0 CB B:MET7 4.2 31.9 1.0 C2A B:HEM151 4.2 32.8 1.0 CG B:HIS102 4.2 40.6 1.0 C2B B:HEM151 4.3 30.3 1.0 C3B B:HEM151 4.4 30.3 1.0 C3C B:HEM151 4.4 27.5 1.0 C2C B:HEM151 4.4 28.9 1.0

Iron binding site 3 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


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 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe152 b:33.8 occ:1.00 FE C:HEM152 0.0 33.8 1.0 NB C:HEM152 1.9 32.6 1.0 NA C:HEM152 2.0 36.0 1.0 ND C:HEM152 2.1 37.0 1.0 NE2 C:HIS102 2.1 37.0 1.0 NC C:HEM152 2.1 32.3 1.0 SD C:MET7 2.4 28.8 1.0 CE1 C:HIS102 2.9 37.4 1.0 C1B C:HEM152 2.9 33.4 1.0 C4A C:HEM152 2.9 35.7 1.0 C4B C:HEM152 3.0 29.7 1.0 C1A C:HEM152 3.1 38.3 1.0 C1C C:HEM152 3.1 29.8 1.0 C4D C:HEM152 3.1 38.1 1.0 C1D C:HEM152 3.2 38.2 1.0 C4C C:HEM152 3.2 33.8 1.0 CHB C:HEM152 3.3 34.4 1.0 CD2 C:HIS102 3.3 36.9 1.0 CHC C:HEM152 3.4 30.3 1.0 CHA C:HEM152 3.4 37.3 1.0 CHD C:HEM152 3.5 36.5 1.0 CG C:MET7 3.6 33.7 1.0 CE C:MET7 3.6 29.9 1.0 ND1 C:HIS102 4.1 40.3 1.0 C2B C:HEM152 4.1 33.8 1.0 C3B C:HEM152 4.2 31.9 1.0 C3A C:HEM152 4.2 38.8 1.0 CB C:MET7 4.2 36.1 1.0 C2A C:HEM152 4.3 39.9 1.0 CG C:HIS102 4.3 38.3 1.0 C3D C:HEM152 4.4 42.5 1.0 C2D C:HEM152 4.4 41.2 1.0 C2C C:HEM152 4.4 31.2 1.0 C3C C:HEM152 4.4 31.9 1.0 CA C:MET7 5.0 39.1 1.0

Iron binding site 4 out of 4 in the Crystal Structure of A 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules


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 16-Helix Bundle Architecture Produced By the Zinc-Mediated Self Assembly of Four Cytochrome CB562 Molecules within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe153 b:37.3 occ:1.00 FE D:HEM153 0.0 37.3 1.0 NE2 D:HIS102 1.9 39.8 1.0 ND D:HEM153 1.9 34.4 1.0 NB D:HEM153 2.0 32.7 1.0 NA D:HEM153 2.0 37.5 1.0 NC D:HEM153 2.1 34.9 1.0 SD D:MET7 2.5 31.2 1.0 CE1 D:HIS102 2.7 42.8 1.0 C1D D:HEM153 3.0 35.5 1.0 C4D D:HEM153 3.0 36.3 1.0 CD2 D:HIS102 3.0 39.3 1.0 C1B D:HEM153 3.1 32.8 1.0 C4B D:HEM153 3.1 34.4 1.0 C4A D:HEM153 3.1 35.9 1.0 C1A D:HEM153 3.1 38.1 1.0 C4C D:HEM153 3.1 33.5 1.0 C1C D:HEM153 3.1 33.4 1.0 CHA D:HEM153 3.4 35.6 1.0 CHD D:HEM153 3.4 34.8 1.0 CHB D:HEM153 3.4 33.4 1.0 CHC D:HEM153 3.4 33.3 1.0 CE D:MET7 3.6 30.1 1.0 CG D:MET7 3.6 35.5 1.0 ND1 D:HIS102 3.9 42.3 1.0 CG D:HIS102 4.1 40.1 1.0 C2D D:HEM153 4.2 37.2 1.0 C3D D:HEM153 4.2 38.2 1.0 C3A D:HEM153 4.3 38.3 1.0 C2B D:HEM153 4.3 33.2 1.0 C3B D:HEM153 4.3 34.3 1.0 C2C D:HEM153 4.3 32.7 1.0 C3C D:HEM153 4.3 32.8 1.0 C2A D:HEM153 4.4 40.9 1.0 CB D:MET7 4.4 35.4 1.0

E.N.Salgado, J.Faraone-Mennella, F.A.Tezcan. Controlling Protein-Protein Interactions Through Metal Coordination: Assembly of A 16-Helix Bundle Protein. J.Am.Chem.Soc. V. 129 13374 2007.
ISSN: ISSN 0002-7863
PubMed: 17929927
DOI: 10.1021/JA075261O