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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2b11:

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

Zinc Binding Sites:

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 2b11

Go back to Zinc Binding Sites List in 2b11
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 2b11

Go back to Zinc Binding Sites List in 2b11
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

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 Dec 16 03:18:01 2020

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