Iron in PDB 2b11: Crystal Structure of the Protein-Protein Complex Between F82W Cytochrome C and Cytochrome C Peroxidase

All present enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82W Cytochrome C and Cytochrome C Peroxidase:
1.11.1.5;

The structure of Crystal Structure of the Protein-Protein Complex Between F82W Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b11 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)	30.00 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.884, 117.864, 88.470, 90.00, 104.23, 90.00
R / Rfree (%)	26.5 / 29.3

The structure of Crystal Structure of the Protein-Protein Complex Between F82W 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 F82W Cytochrome C and Cytochrome C Peroxidase (pdb code 2b11). 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 F82W Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b11:
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 F82W 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 F82W Cytochrome C and Cytochrome C Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1201 b:12.5 occ:1.00 FE C:HEM1201 0.0 12.5 1.0 NB C:HEM1201 2.0 11.9 1.0 ND C:HEM1201 2.0 3.1 1.0 NA C:HEM1201 2.0 10.4 1.0 NC C:HEM1201 2.1 2.0 1.0 NE2 C:HIS675 2.3 17.0 1.0 O C:HOH1402 3.0 16.3 1.0 C1D C:HEM1201 3.1 9.8 1.0 C1B C:HEM1201 3.1 16.1 1.0 C4D C:HEM1201 3.1 12.4 1.0 C1C C:HEM1201 3.1 3.4 1.0 C4A C:HEM1201 3.1 10.5 1.0 C4B C:HEM1201 3.1 13.1 1.0 C4C C:HEM1201 3.1 8.9 1.0 C1A C:HEM1201 3.1 11.9 1.0 CD2 C:HIS675 3.1 8.8 1.0 CE1 C:HIS675 3.3 22.6 1.0 CHD C:HEM1201 3.4 11.1 1.0 CHB C:HEM1201 3.4 12.1 1.0 CHC C:HEM1201 3.4 16.2 1.0 CHA C:HEM1201 3.4 16.3 1.0 O C:HOH1878 3.8 39.7 1.0 C3D C:HEM1201 4.3 10.1 1.0 C2D C:HEM1201 4.3 13.6 1.0 C2B C:HEM1201 4.3 10.0 1.0 NE1 C:TRP551 4.3 7.7 1.0 C2A C:HEM1201 4.3 3.4 1.0 C3A C:HEM1201 4.3 5.6 1.0 CG C:HIS675 4.3 24.1 1.0 C2C C:HEM1201 4.3 4.5 1.0 C3B C:HEM1201 4.4 7.6 1.0 ND1 C:HIS675 4.4 19.8 1.0 C3C C:HEM1201 4.4 9.1 1.0 CD1 C:TRP551 4.7 9.3 1.0 CH2 C:TRP691 5.0 4.8 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Protein-Protein Complex Between F82W 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 F82W Cytochrome C and Cytochrome C Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1301 b:31.0 occ:1.00 FE D:HEM1301 0.0 31.0 1.0 NA D:HEM1301 2.0 43.6 1.0 NB D:HEM1301 2.0 39.1 1.0 ND D:HEM1301 2.1 46.7 1.0 NE2 D:HIS818 2.1 35.0 1.0 SD D:MET880 2.1 36.5 1.0 NC D:HEM1301 2.1 44.2 1.0 CE1 D:HIS818 2.9 36.8 1.0 C4A D:HEM1301 3.0 40.3 1.0 C1A D:HEM1301 3.0 35.6 1.0 C1B D:HEM1301 3.0 42.0 1.0 C4B D:HEM1301 3.0 39.6 1.0 C4D D:HEM1301 3.1 45.8 1.0 C1C D:HEM1301 3.1 33.0 1.0 C1D D:HEM1301 3.1 43.2 1.0 CE D:MET880 3.1 25.0 1.0 C4C D:HEM1301 3.2 41.6 1.0 CD2 D:HIS818 3.2 36.0 1.0 CHA D:HEM1301 3.3 38.5 1.0 CHB D:HEM1301 3.3 42.6 1.0 CHC D:HEM1301 3.4 33.6 1.0 CHD D:HEM1301 3.5 44.8 1.0 CG D:MET880 3.7 35.3 1.0 ND1 D:HIS818 4.1 36.2 1.0 C2B D:HEM1301 4.3 36.1 1.0 C3A D:HEM1301 4.3 40.5 1.0 CG D:HIS818 4.3 38.1 1.0 C3B D:HEM1301 4.3 40.0 1.0 C2A D:HEM1301 4.3 39.0 1.0 C3D D:HEM1301 4.4 45.0 1.0 C2D D:HEM1301 4.4 43.6 1.0 C2C D:HEM1301 4.4 41.5 1.0 C3C D:HEM1301 4.4 38.4 1.0 CB D:MET880 4.6 40.8 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