Zinc 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:

Iron

(Fe)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Protein-Protein Complex Between F82W Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b11:
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 F82W 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 F82W Cytochrome C and Cytochrome C Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:16.3 occ:1.00 ZN A:ZNH1001 0.0 16.3 1.0 NA A:ZNH1001 2.0 10.6 1.0 ND A:ZNH1001 2.0 6.9 1.0 NB A:ZNH1001 2.0 14.1 1.0 NC A:ZNH1001 2.1 5.2 1.0 NE2 A:HIS175 2.2 12.1 1.0 O A:HOH1401 2.9 16.0 1.0 C1A A:ZNH1001 3.0 13.3 1.0 C4D A:ZNH1001 3.0 15.5 1.0 C1D A:ZNH1001 3.0 15.0 1.0 C4A A:ZNH1001 3.1 21.1 1.0 CD2 A:HIS175 3.1 7.7 1.0 C1B A:ZNH1001 3.1 20.7 1.0 C4C A:ZNH1001 3.1 7.4 1.0 C1C A:ZNH1001 3.1 8.0 1.0 C4B A:ZNH1001 3.1 20.4 1.0 CE1 A:HIS175 3.2 17.1 1.0 CHA A:ZNH1001 3.3 14.7 1.0 CHB A:ZNH1001 3.4 22.5 1.0 CHD A:ZNH1001 3.4 15.8 1.0 CHC A:ZNH1001 3.5 9.0 1.0 C2A A:ZNH1001 4.2 9.8 1.0 CG A:HIS175 4.2 20.2 1.0 ND1 A:HIS175 4.3 18.8 1.0 C3D A:ZNH1001 4.3 15.0 1.0 C2D A:ZNH1001 4.3 17.7 1.0 C3A A:ZNH1001 4.3 8.8 1.0 C2B A:ZNH1001 4.3 21.4 1.0 NE1 A:TRP51 4.3 9.1 1.0 C3C A:ZNH1001 4.4 9.1 1.0 C2C A:ZNH1001 4.4 9.8 1.0 C3B A:ZNH1001 4.4 22.5 1.0 O A:HOH1585 4.4 0.7 1.0 CD1 A:TRP51 4.9 5.2 1.0 CH2 A:TRP191 4.9 13.6 1.0

Zinc 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 Zinc with other atoms in the Zn 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 B:Zn1101 b:28.8 occ:1.00 ZN B:ZNH1101 0.0 28.8 1.0 SD B:MET380 2.1 23.1 1.0 ND B:ZNH1101 2.1 39.3 1.0 NB B:ZNH1101 2.1 36.5 1.0 NC B:ZNH1101 2.1 36.2 1.0 NA B:ZNH1101 2.1 30.9 1.0 NE2 B:HIS318 2.1 23.1 1.0 CE1 B:HIS318 2.9 37.5 1.0 C4D B:ZNH1101 3.0 35.7 1.0 C4B B:ZNH1101 3.1 36.6 1.0 C1C B:ZNH1101 3.1 31.6 1.0 C1A B:ZNH1101 3.1 32.0 1.0 C1D B:ZNH1101 3.1 31.2 1.0 C4C B:ZNH1101 3.1 36.4 1.0 C1B B:ZNH1101 3.1 39.3 1.0 C4A B:ZNH1101 3.1 33.9 1.0 CD2 B:HIS318 3.3 34.0 1.0 CHA B:ZNH1101 3.3 32.4 1.0 CHC B:ZNH1101 3.4 27.4 1.0 CE B:MET380 3.4 31.9 1.0 CHD B:ZNH1101 3.5 34.5 1.0 CG B:MET380 3.5 24.9 1.0 CHB B:ZNH1101 3.5 36.2 1.0 O B:HOH1840 3.9 52.1 1.0 ND1 B:HIS318 4.1 31.3 1.0 CG B:HIS318 4.3 29.8 1.0 C3D B:ZNH1101 4.3 43.3 1.0 C3B B:ZNH1101 4.3 41.0 1.0 C2D B:ZNH1101 4.3 32.1 1.0 C2B B:ZNH1101 4.3 33.6 1.0 C2C B:ZNH1101 4.3 38.6 1.0 C2A B:ZNH1101 4.4 33.6 1.0 C3C B:ZNH1101 4.4 36.2 1.0 C3A B:ZNH1101 4.4 36.4 1.0 CB B:MET380 4.4 28.2 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