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Iron in PDB 4zf8: Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone

Enzymatic activity of Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone

All present enzymatic activity of Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone:
1.14.14.1; 1.6.2.4;

Protein crystallography data

The structure of Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone, PDB code: 4zf8 was solved by W.E.Rogers, T.Othman, D.K.Heidary, T.Huxford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.41 / 2.77
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 55.899, 55.899, 711.033, 90.00, 90.00, 120.00
R / Rfree (%) 21.5 / 26.3

Other elements in 4zf8:

The structure of Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone also contains other interesting chemical elements:

Nickel (Ni) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone (pdb code 4zf8). 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 Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone, PDB code: 4zf8:

Iron binding site 1 out of 1 in 4zf8

Go back to Iron Binding Sites List in 4zf8
Iron binding site 1 out of 1 in the Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 Pentamutant From BM3 with Bound Metyrapone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:37.8
occ:1.00
FE A:HEM501 0.0 37.8 1.0
NC A:HEM501 2.0 40.5 1.0
NB A:HEM501 2.0 43.0 1.0
NA A:HEM501 2.1 43.5 1.0
ND A:HEM501 2.1 46.1 1.0
SG A:CYS400 2.4 43.2 1.0
N14 A:MYT502 2.6 46.6 1.0
C4C A:HEM501 3.0 42.0 1.0
C1C A:HEM501 3.0 41.4 1.0
C4B A:HEM501 3.1 41.7 1.0
C1B A:HEM501 3.1 47.2 1.0
C1D A:HEM501 3.1 43.0 1.0
C4A A:HEM501 3.1 47.0 1.0
C1A A:HEM501 3.1 47.6 1.0
C4D A:HEM501 3.1 42.4 1.0
CB A:CYS400 3.2 45.8 1.0
C13 A:MYT502 3.4 49.3 1.0
CHD A:HEM501 3.4 44.3 1.0
CHC A:HEM501 3.4 41.2 1.0
CHB A:HEM501 3.4 47.3 1.0
CHA A:HEM501 3.4 43.9 1.0
C15 A:MYT502 3.6 42.6 1.0
CA A:CYS400 4.0 45.4 1.0
C3C A:HEM501 4.2 41.3 1.0
C2C A:HEM501 4.2 44.2 1.0
C2B A:HEM501 4.3 44.8 1.0
C3B A:HEM501 4.3 43.1 1.0
C3A A:HEM501 4.3 47.7 1.0
C2A A:HEM501 4.3 48.4 1.0
C2D A:HEM501 4.3 40.3 1.0
C3D A:HEM501 4.3 44.0 1.0
C12 A:MYT502 4.7 55.8 1.0
C16 A:MYT502 4.8 46.5 1.0
C A:CYS400 4.8 46.0 1.0
N A:ILE401 4.9 44.1 1.0
N A:GLY402 4.9 46.3 1.0

Reference:

I.Geronimo, C.A.Denning, W.E.Rogers, T.Othman, T.Huxford, D.K.Heidary, E.C.Glazer, C.M.Payne. Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants. Biochemistry V. 55 3594 2016.
ISSN: ISSN 0006-2960
PubMed: 27267136
DOI: 10.1021/ACS.BIOCHEM.6B00183
Page generated: Mon Aug 5 18:11:35 2024

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