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Iron in PDB 5cpp: The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam)

Enzymatic activity of The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam)

All present enzymatic activity of The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam):
1.14.15.1;

Protein crystallography data

The structure of The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam), PDB code: 5cpp was solved by R.Raag, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.08
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 108.670, 103.900, 36.380, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam) (pdb code 5cpp). 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 The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam), PDB code: 5cpp:

Iron binding site 1 out of 1 in 5cpp

Go back to Iron Binding Sites List in 5cpp
Iron binding site 1 out of 1 in the The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450(Cam) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe417

b:9.7
occ:1.00
 FE A:HEM417 0.0 9.7 1.0
ND A:HEM417 2.0 10.7 1.0
NB A:HEM417 2.0 10.5 1.0
SG A:CYS357 2.1 9.1 1.0
NA A:HEM417 2.1 10.7 1.0
NC A:HEM417 2.1 10.8 1.0
C4A A:HEM417 3.0 9.9 1.0
C4C A:HEM417 3.0 10.9 1.0
C1D A:HEM417 3.0 10.9 1.0
C1B A:HEM417 3.1 12.0 1.0
C4D A:HEM417 3.1 11.6 1.0
C4B A:HEM417 3.1 12.1 1.0
C1A A:HEM417 3.1 9.8 1.0
C1C A:HEM417 3.1 10.7 1.0
CB A:CYS357 3.3 12.3 1.0
CHD A:HEM417 3.4 9.8 1.0
CHB A:HEM417 3.4 10.6 1.0
CHA A:HEM417 3.5 9.8 1.0
CHC A:HEM417 3.5 11.4 1.0
CA A:CYS357 4.0 10.1 1.0
C2D A:HEM417 4.2 11.7 1.0
C2B A:HEM417 4.2 12.3 1.0
C3D A:HEM417 4.2 10.4 1.0
C3B A:HEM417 4.3 10.8 1.0
C3C A:HEM417 4.3 13.0 1.0
C2A A:HEM417 4.3 10.4 1.0
C2C A:HEM417 4.3 12.2 1.0
C3A A:HEM417 4.3 11.1 1.0
C5 A:ADO422 4.4 16.3 1.0
C4 A:ADO422 4.5 16.6 1.0
N A:GLY359 4.6 10.2 1.0
C6 A:ADO422 4.6 16.0 1.0
C A:CYS357 4.8 11.1 1.0
CA A:GLY359 4.8 10.9 1.0
N A:LEU358 4.9 10.7 1.0
CD1 A:PHE350 5.0 6.8 1.0

Reference:

R.Raag, T.L.Poulos. The Structural Basis For Substrate-Induced Changes in Redox Potential and Spin Equilibrium in Cytochrome P-450CAM. Biochemistry V. 28 917 1989.
ISSN: ISSN 0006-2960
PubMed: 2713354
DOI: 10.1021/BI00428A077
Page generated: Mon Aug 5 21:35:38 2024

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