Magnesium in PDB 8sf4: Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form

All present enzymatic activity of Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form:
4.4.1.1;

The structure of Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form, PDB code: 8sf4 was solved by L.J.Perkins, A.R.Buller, C.A.Bindman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.46
Space group	P 2 3
Cell size a, b, c (Å), α, β, γ (°)	117.591, 117.591, 117.591, 90, 90, 90
R / Rfree (%)	13.3 / 14.8

The binding sites of Magnesium atom in the Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form (pdb code 8sf4). 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 Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form, PDB code: 8sf4:

Magnesium binding site 1 out of 1 in the Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cystathionine Gamma Lyase From Thermobifida Fusca in Internal Aldimine Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:32.4 occ:1.00 O A:HOH550 2.1 26.5 1.0 O A:HOH832 2.1 33.5 1.0 O A:HOH667 2.1 35.4 1.0 O A:HOH856 3.7 44.5 1.0 O A:ALA17 4.2 19.3 1.0 O A:HOH818 4.3 43.2 1.0 O A:HOH523 4.5 24.3 1.0 O A:GLU16 4.5 20.4 1.0 N A:ALA19 4.6 19.1 1.0 O A:HOH736 4.6 32.5 1.0 O A:HOH636 4.6 40.1 1.0 CB A:GLU16 4.6 24.9 1.0 OE1 A:GLU16 4.8 52.3 1.0 CB A:ALA19 4.9 22.8 1.0 CA A:ASP18 5.0 17.4 1.0 C A:ALA17 5.0 17.7 1.0

A.P.Zmich, L.J.Perkins, C.A.Bingman, A.R.Buller. Multiplexed Deconvolution of Enzyme Function in A Plp-Dependent Protein Family To Be Published.