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Iron in PDB 1p7r: Crystal Structure of Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine

Enzymatic activity of Crystal Structure of Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine

All present enzymatic activity of Crystal Structure of Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structure of Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine, PDB code: 1p7r was solved by M.Strickler, B.M.Goldstein, K.Maxfield, L.Shireman, G.Kim, D.Matteson, J.P.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.38 / 2.85
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 63.455, 63.455, 248.759, 90.00, 90.00, 90.00
R / Rfree (%) 23.8 / 28.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine (pdb code 1p7r). 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 Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine, PDB code: 1p7r:

Iron binding site 1 out of 1 in 1p7r

Go back to Iron Binding Sites List in 1p7r
Iron binding site 1 out of 1 in the Crystal Structure of Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine


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 Reduced, Co-Exposed Complex of Cytochrome P450CAM with (S)-(-)-Nicotine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe430

b:27.3
occ:1.00
 FE A:HEM430 0.0 27.3 1.0
NC A:HEM430 1.9 25.6 1.0
NB A:HEM430 2.0 26.6 1.0
NA A:HEM430 2.0 24.7 1.0
ND A:HEM430 2.0 25.4 1.0
SG A:CYS357 2.4 25.4 1.0
C1C A:HEM430 3.0 26.2 1.0
C4C A:HEM430 3.0 25.5 1.0
C4B A:HEM430 3.0 26.6 1.0
C4A A:HEM430 3.0 23.2 1.0
C1B A:HEM430 3.0 25.0 1.0
C1D A:HEM430 3.1 23.9 1.0
C1A A:HEM430 3.1 23.8 1.0
C4D A:HEM430 3.1 23.8 1.0
CHC A:HEM430 3.3 27.1 1.0
CHD A:HEM430 3.4 23.8 1.0
CHB A:HEM430 3.4 23.7 1.0
CHA A:HEM430 3.4 24.1 1.0
CB A:CYS357 3.6 26.0 1.0
C8 A:NCT440 4.1 9.7 1.0
C2C A:HEM430 4.2 26.6 1.0
C3C A:HEM430 4.3 26.2 1.0
C3B A:HEM430 4.3 25.5 1.0
C3A A:HEM430 4.3 22.4 1.0
C2B A:HEM430 4.3 24.7 1.0
C2A A:HEM430 4.3 21.5 1.0
C2D A:HEM430 4.3 22.9 1.0
C3D A:HEM430 4.3 22.6 1.0
CA A:CYS357 4.3 26.5 1.0
N A:GLY359 4.7 25.3 1.0
C9 A:NCT440 4.8 6.6 1.0
N A:LEU358 5.0 26.3 1.0

Reference:

M.Strickler, B.M.Goldstein, K.Maxfield, L.Shireman, G.Kim, D.Matteson, J.P.Jones. Crystallographic Studies on the Complex Behavior of Nicotine Binding to P450CAM (CYP101)(Dagger). Biochemistry V. 42 11943 2003.
ISSN: ISSN 0006-2960
PubMed: 14556625
DOI: 10.1021/BI034833O
Page generated: Sun Dec 13 14:27:49 2020

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