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Iron in PDB 1u75: Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase

Enzymatic activity of Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase

All present enzymatic activity of Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase, PDB code: 1u75 was solved by B.R.Crane, S.A.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 104.465, 104.465, 186.884, 90.00, 90.00, 90.00
R / Rfree (%) 27.1 / 30.6

Other elements in 1u75:

The structure of Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase (pdb code 1u75). 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 Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase, PDB code: 1u75:

Iron binding site 1 out of 1 in 1u75

Go back to Iron Binding Sites List in 1u75
Iron binding site 1 out of 1 in the Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted 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 Electron Transfer Complex Between Horse Heart Cytochrome C and Zinc- Porphyrin Substituted Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1101

b:47.0
occ:1.00
 FE B:HEM1101 0.0 47.0 1.0
NC B:HEM1101 2.0 49.3 1.0
NA B:HEM1101 2.0 48.7 1.0
NE2 B:HIS18 2.0 51.2 1.0
NB B:HEM1101 2.1 48.6 1.0
ND B:HEM1101 2.1 51.0 1.0
SD B:MET80 2.7 66.3 1.0
CD2 B:HIS18 3.0 50.4 1.0
C1A B:HEM1101 3.0 52.2 1.0
C4D B:HEM1101 3.0 54.8 1.0
C1C B:HEM1101 3.0 50.1 1.0
C4C B:HEM1101 3.1 50.4 1.0
C4B B:HEM1101 3.1 50.0 1.0
C1B B:HEM1101 3.1 45.9 1.0
CE1 B:HIS18 3.1 51.1 1.0
C4A B:HEM1101 3.1 47.8 1.0
C1D B:HEM1101 3.1 54.1 1.0
CHA B:HEM1101 3.3 53.5 1.0
CHC B:HEM1101 3.4 50.0 1.0
CHD B:HEM1101 3.4 52.5 1.0
CHB B:HEM1101 3.4 48.4 1.0
CE B:MET80 3.8 69.3 1.0
CG B:MET80 3.9 66.7 1.0
CG B:HIS18 4.1 52.4 1.0
ND1 B:HIS18 4.2 51.1 1.0
C2A B:HEM1101 4.3 53.0 1.0
C2C B:HEM1101 4.3 51.9 1.0
C2B B:HEM1101 4.3 49.3 1.0
C3B B:HEM1101 4.3 49.5 1.0
C3A B:HEM1101 4.3 51.0 1.0
C3C B:HEM1101 4.3 52.0 1.0
C3D B:HEM1101 4.3 54.8 1.0
C2D B:HEM1101 4.4 56.2 1.0
CB B:MET80 4.7 66.2 1.0

Reference:

S.A.Kang, P.J.Marjavaara, B.R.Crane. Electron Transfer Between Cytochrome C and Cytochome C Peroxidase in Single Crystals. J.Am.Chem.Soc. V. 126 10836 2004.
ISSN: ISSN 0002-7863
PubMed: 15339156
DOI: 10.1021/JA049230U
Page generated: Sat Aug 3 15:24:50 2024

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