Magnesium in PDB 7reh: Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid

Protein crystallography data

The structure of Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid, PDB code: 7reh was solved by M.N.Podgorski, J.B.Bruning, S.G.Bell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.22 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.31, 51.51, 79.65, 90, 92.21, 90
R / Rfree (%) 17.1 / 20.3

Other elements in 7reh:

The structure of Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Iron (Fe) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid (pdb code 7reh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid, PDB code: 7reh:

Magnesium binding site 1 out of 1 in 7reh

Go back to Magnesium Binding Sites List in 7reh
Magnesium binding site 1 out of 1 in the Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of T252E CYP199A4 Bound to 4-Methoxybenzoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:18.4
occ:1.00
O A:HOH794 2.1 19.1 1.0
O A:HOH817 2.1 18.2 1.0
O A:HOH951 2.2 24.8 1.0
O A:HOH890 3.7 26.4 1.0
O A:LEU166 4.1 11.6 1.0
O A:ACT505 4.2 20.6 1.0
O A:HOH832 4.3 22.1 1.0
CA A:LYS167 4.5 8.6 1.0
O A:HOH934 4.5 15.3 1.0
N A:GLN168 4.8 10.8 1.0
NE2 A:GLN168 4.8 25.9 1.0
C A:LEU166 4.9 9.6 1.0
C A:LYS167 5.0 9.5 1.0
CG A:GLN168 5.0 19.9 1.0

Reference:

M.N.Podgorski, J.S.Harbort, J.H.Z.Lee, G.T.Nguyen, J.B.Bruning, W.A.Donald, P.V.Bernhardt, J.R.Harmer, S.G.Bell. An Altered Heme Environment in An Engineered Cytochrome P450 Enzyme Enables the Switch From Monooxygenase to Peroxygenase Activity Acs Catalysis 1614 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C05877
Page generated: Thu Oct 3 07:50:40 2024

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