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Zinc in PDB 2b12: Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase

Enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase

All present enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b12 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 / 3.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.789, 51.832, 183.645, 90.00, 90.00, 90.00
R / Rfree (%) 27.7 / 26.8

Other elements in 2b12:

The structure of Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase also contains other interesting chemical elements:

Iron (Fe) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase (pdb code 2b12). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Protein-Protein Complex Between F82Y Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b12:

Zinc binding site 1 out of 1 in 2b12

Go back to Zinc Binding Sites List in 2b12
Zinc binding site 1 out of 1 in the Crystal Structure of the Protein-Protein Complex Between F82Y 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 F82Y Cytochrome C and Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn295

b:2.0
occ:1.00
 ZN A:ZNH295 0.0 2.0 1.0
NE2 A:HIS175 1.9 2.0 1.0
ND A:ZNH295 2.0 2.0 1.0
NC A:ZNH295 2.1 2.0 1.0
NA A:ZNH295 2.1 2.0 1.0
NB A:ZNH295 2.1 2.0 1.0
CD2 A:HIS175 2.8 2.0 1.0
C1D A:ZNH295 3.0 2.0 1.0
CE1 A:HIS175 3.0 2.0 1.0
C4D A:ZNH295 3.0 2.0 1.0
C4C A:ZNH295 3.1 2.0 1.0
C1B A:ZNH295 3.1 2.0 1.0
C1A A:ZNH295 3.1 2.0 1.0
C1C A:ZNH295 3.1 2.0 1.0
C4A A:ZNH295 3.1 2.0 1.0
C4B A:ZNH295 3.1 2.0 1.0
CHD A:ZNH295 3.3 2.0 1.0
CHC A:ZNH295 3.4 2.0 1.0
CHA A:ZNH295 3.4 2.0 1.0
CHB A:ZNH295 3.4 2.0 1.0
CG A:HIS175 4.0 2.0 1.0
ND1 A:HIS175 4.0 2.0 1.0
C2D A:ZNH295 4.1 2.0 1.0
C3D A:ZNH295 4.2 3.2 1.0
NE1 A:TRP51 4.3 2.0 1.0
C2A A:ZNH295 4.3 2.0 1.0
C2B A:ZNH295 4.3 2.0 1.0
C3A A:ZNH295 4.3 2.0 1.0
C3C A:ZNH295 4.3 2.0 1.0
C2C A:ZNH295 4.3 2.0 1.0
C3B A:ZNH295 4.3 2.0 1.0
CD1 A:TRP51 4.7 2.0 1.0
CH2 A:TRP191 4.8 2.0 1.0
CZ2 A:TRP191 4.9 2.0 1.0

Reference:

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
Page generated: Wed Oct 16 21:53:11 2024

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