Iron in PDB 2b10: Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase

All present enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase:
1.11.1.5;

The structure of Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b10 was solved by S.A.Kang, B.R.Crane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.575, 113.448, 88.002, 90.00, 104.55, 90.00
R / Rfree (%)	28.4 / 30.6

The structure of Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase (pdb code 2b10). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b10:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase


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 the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe409 b:2.0 occ:1.00 FE B:HEM409 0.0 2.0 1.0 NB B:HEM409 2.0 2.0 1.0 ND B:HEM409 2.1 2.0 1.0 NA B:HEM409 2.1 2.0 1.0 NC B:HEM409 2.1 2.0 1.0 NE2 B:HIS18 2.4 9.1 1.0 C1D B:HEM409 3.0 2.0 1.0 C4B B:HEM409 3.0 2.0 1.0 C1B B:HEM409 3.0 2.0 1.0 CE1 B:HIS18 3.0 12.3 1.0 SD B:MET80 3.1 17.2 1.0 C4D B:HEM409 3.1 2.0 1.0 C4C B:HEM409 3.1 2.0 1.0 C4A B:HEM409 3.1 2.0 1.0 C1C B:HEM409 3.1 2.0 1.0 C1A B:HEM409 3.1 2.0 1.0 CE B:MET80 3.3 16.8 1.0 CHD B:HEM409 3.3 2.0 1.0 CHC B:HEM409 3.4 2.0 1.0 CHB B:HEM409 3.4 2.0 1.0 CHA B:HEM409 3.5 2.0 1.0 CD2 B:HIS18 3.6 13.0 1.0 CG B:MET80 4.1 17.4 1.0 C3B B:HEM409 4.2 2.0 1.0 C2B B:HEM409 4.2 2.0 1.0 C2D B:HEM409 4.2 2.0 1.0 ND1 B:HIS18 4.3 13.6 1.0 C3D B:HEM409 4.3 2.0 1.0 C3A B:HEM409 4.3 2.0 1.0 C2A B:HEM409 4.4 2.0 1.0 C3C B:HEM409 4.4 2.0 1.0 C2C B:HEM409 4.4 2.0 1.0 CG B:HIS18 4.5 14.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase


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 the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe909 b:9.2 occ:1.00 FE D:HEM909 0.0 9.2 1.0 NB D:HEM909 2.0 10.9 1.0 NE2 D:HIS18 2.0 15.8 1.0 NC D:HEM909 2.1 7.0 1.0 ND D:HEM909 2.1 7.0 1.0 NA D:HEM909 2.1 6.8 1.0 SD D:MET80 2.3 15.3 1.0 CD2 D:HIS18 3.0 15.7 1.0 CE1 D:HIS18 3.1 18.5 1.0 C1B D:HEM909 3.1 7.6 1.0 C4B D:HEM909 3.1 10.1 1.0 C1D D:HEM909 3.1 5.5 1.0 C4C D:HEM909 3.1 6.4 1.0 C4A D:HEM909 3.1 6.0 1.0 C1C D:HEM909 3.1 6.8 1.0 C4D D:HEM909 3.1 6.0 1.0 C1A D:HEM909 3.1 11.6 1.0 CHD D:HEM909 3.4 5.5 1.0 CHB D:HEM909 3.4 5.8 1.0 CHC D:HEM909 3.4 9.1 1.0 CHA D:HEM909 3.4 5.8 1.0 CE D:MET80 3.4 13.6 1.0 CG D:MET80 3.7 13.3 1.0 CG D:HIS18 4.1 16.3 1.0 ND1 D:HIS18 4.1 17.6 1.0 C2B D:HEM909 4.3 7.2 1.0 C3B D:HEM909 4.3 13.7 1.0 C2D D:HEM909 4.3 6.1 1.0 C3A D:HEM909 4.3 5.0 1.0 C2C D:HEM909 4.3 3.3 1.0 C2A D:HEM909 4.3 8.6 1.0 C3D D:HEM909 4.3 4.4 1.0 C3C D:HEM909 4.3 4.8 1.0 CB D:MET80 4.6 16.5 1.0 OH D:TYR67 4.8 13.0 1.0

S.A.Kang, B.R.Crane. Effects of Interface Mutations on Association Modes and Electron-Transfer Rates Between Proteins Proc.Natl.Acad.Sci.Usa V. 102 15465 2005.
ISSN: ISSN 0027-8424
PubMed: 16227441
DOI: 10.1073/PNAS.0505176102