Zinc 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:

Iron

(Fe)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Protein-Protein Complex Between F82S Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b10:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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 A:Zn295 b:13.2 occ:1.00 ZN A:ZNH295 0.0 13.2 1.0 ND A:ZNH295 2.0 12.5 1.0 NB A:ZNH295 2.0 15.4 1.0 NA A:ZNH295 2.1 18.9 1.0 NE2 A:HIS175 2.1 21.3 1.0 NC A:ZNH295 2.1 16.8 1.0 C4D A:ZNH295 3.0 12.9 1.0 C1D A:ZNH295 3.0 11.1 1.0 CD2 A:HIS175 3.0 16.4 1.0 C1B A:ZNH295 3.0 8.8 1.0 C1A A:ZNH295 3.1 19.9 1.0 C4C A:ZNH295 3.1 18.1 1.0 C4B A:ZNH295 3.1 7.2 1.0 C4A A:ZNH295 3.1 14.7 1.0 CE1 A:HIS175 3.1 27.4 1.0 C1C A:ZNH295 3.1 15.3 1.0 CHA A:ZNH295 3.3 15.6 1.0 CHD A:ZNH295 3.4 8.1 1.0 CHB A:ZNH295 3.4 14.0 1.0 CHC A:ZNH295 3.4 14.4 1.0 CG A:HIS175 4.2 17.5 1.0 ND1 A:HIS175 4.2 21.7 1.0 C2D A:ZNH295 4.3 6.9 1.0 C2A A:ZNH295 4.3 15.0 1.0 C3D A:ZNH295 4.3 13.9 1.0 C3A A:ZNH295 4.3 19.4 1.0 C2B A:ZNH295 4.3 10.6 1.0 C2C A:ZNH295 4.3 16.2 1.0 C3C A:ZNH295 4.3 19.3 1.0 C3B A:ZNH295 4.4 9.2 1.0 NE1 A:TRP51 4.4 8.0 1.0 CD1 A:TRP51 4.8 14.1 1.0 CH2 A:TRP191 4.9 9.2 1.0 CZ2 A:TRP191 4.9 6.1 1.0

Zinc 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 Zinc with other atoms in the Zn 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 C:Zn795 b:11.6 occ:1.00 ZN C:ZNH795 0.0 11.6 1.0 ND C:ZNH795 2.0 12.4 1.0 NC C:ZNH795 2.0 12.2 1.0 NB C:ZNH795 2.1 18.3 1.0 NA C:ZNH795 2.1 18.2 1.0 NE2 C:HIS175 2.2 15.2 1.0 CD2 C:HIS175 3.0 15.5 1.0 C1D C:ZNH795 3.0 3.2 1.0 C4C C:ZNH795 3.0 17.1 1.0 C1C C:ZNH795 3.0 13.3 1.0 C4D C:ZNH795 3.1 11.5 1.0 C4B C:ZNH795 3.1 15.1 1.0 C1A C:ZNH795 3.1 15.7 1.0 C1B C:ZNH795 3.1 19.4 1.0 C4A C:ZNH795 3.2 19.4 1.0 CE1 C:HIS175 3.3 19.5 1.0 CHD C:ZNH795 3.3 2.9 1.0 CHC C:ZNH795 3.4 17.1 1.0 CHA C:ZNH795 3.4 10.2 1.0 CHB C:ZNH795 3.5 18.6 1.0 NE1 C:TRP51 4.2 8.4 1.0 CG C:HIS175 4.2 18.2 1.0 C2D C:ZNH795 4.3 3.9 1.0 C2A C:ZNH795 4.3 20.4 1.0 ND1 C:HIS175 4.3 16.6 1.0 C3D C:ZNH795 4.3 5.4 1.0 C2C C:ZNH795 4.3 10.0 1.0 C3A C:ZNH795 4.3 21.7 1.0 C3C C:ZNH795 4.4 15.1 1.0 C2B C:ZNH795 4.4 16.7 1.0 C3B C:ZNH795 4.4 21.9 1.0 CD1 C:TRP51 4.7 9.6 1.0 CH2 C:TRP191 4.9 29.5 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