Magnesium in PDB 8w1q: Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa

Enzymatic activity of Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa

All present enzymatic activity of Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa:
1.3.3.11;

Protein crystallography data

The structure of Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa, PDB code: 8w1q was solved by M.E.Walker, T.L.Grove, B.Li, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.57 / 1.56
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.461, 83.551, 68.829, 90, 97.7, 90
R / Rfree (%) 17.6 / 20.8

Other elements in 8w1q:

The structure of Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Potassium (K) 2 atoms
Iron (Fe) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa (pdb code 8w1q). 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 Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa, PDB code: 8w1q:

Magnesium binding site 1 out of 1 in 8w1q

Go back to Magnesium Binding Sites List in 8w1q
Magnesium binding site 1 out of 1 in the Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Aerobic Crystal Structure of Iron-Bound Flcd From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:56.9
occ:1.00
O A:HOH549 2.9 29.7 1.0
O A:LEU259 3.8 26.8 1.0
C A:LEU259 4.7 25.9 1.0

Reference:

W.C.Simke, M.E.Walker, L.A.Calderone, A.T.Putz, J.B.Patteson, C.N.Vitro, C.F.Zizola, M.R.Redinbo, M.E.Pandelia, T.L.Grove, B.Li. Structural Basis For Methine Excision By A Heme Oxygenase-Like Enzyme Acs Cent.Sci. 2024.
ISSN: ESSN 2374-7951
DOI: 10.1021/ACSCENTSCI.4C00015
Page generated: Fri Oct 4 22:16:18 2024

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