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Iron in PDB 2b0z: Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase

Enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase

All present enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b0z 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 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.802, 51.989, 183.669, 90.00, 90.00, 90.00
R / Rfree (%) 26.2 / 28.9

Other elements in 2b0z:

The structure of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase (pdb code 2b0z). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b0z:

Iron binding site 1 out of 1 in 2b0z

Go back to Iron Binding Sites List in 2b0z
Iron binding site 1 out of 1 in the Crystal Structure of the Protein-Protein Complex Between F82I 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 F82I Cytochrome C and Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe109

b:21.6
occ:1.00
 FE B:HEM109 0.0 21.6 1.0
NA B:HEM109 2.0 19.7 1.0
ND B:HEM109 2.0 21.4 1.0
NB B:HEM109 2.0 26.2 1.0
NC B:HEM109 2.0 24.3 1.0
NE2 B:HIS18 2.1 31.5 1.0
SD B:MET80 2.2 24.1 1.0
C4A B:HEM109 3.0 18.0 1.0
C1A B:HEM109 3.0 19.4 1.0
C1C B:HEM109 3.0 24.6 1.0
C1B B:HEM109 3.0 23.1 1.0
C4D B:HEM109 3.0 24.7 1.0
C1D B:HEM109 3.0 15.9 1.0
C4B B:HEM109 3.1 25.6 1.0
C4C B:HEM109 3.1 26.5 1.0
CE1 B:HIS18 3.1 39.4 1.0
CD2 B:HIS18 3.1 32.3 1.0
CE B:MET80 3.3 23.3 1.0
CHB B:HEM109 3.3 19.4 1.0
CHC B:HEM109 3.3 22.2 1.0
CHA B:HEM109 3.3 20.8 1.0
CHD B:HEM109 3.4 23.7 1.0
CG B:MET80 3.5 26.5 1.0
ND1 B:HIS18 4.2 36.9 1.0
C3A B:HEM109 4.2 17.8 1.0
CG B:HIS18 4.2 34.8 1.0
C2A B:HEM109 4.2 17.6 1.0
C2C B:HEM109 4.3 27.4 1.0
C3D B:HEM109 4.3 19.7 1.0
C2D B:HEM109 4.3 18.9 1.0
C2B B:HEM109 4.3 25.1 1.0
C3B B:HEM109 4.3 27.5 1.0
C3C B:HEM109 4.4 23.3 1.0
CB B:MET80 4.4 24.1 1.0
OH B:TYR67 5.0 19.2 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: Sat Aug 3 19:30:41 2024

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