Magnesium in PDB 4pb5: D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate

All present enzymatic activity of D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate:
4.3.1.27;

The structure of D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate, PDB code: 4pb5 was solved by Y.Yasutake, Y.Matsumoto, M.Wada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.46 / 1.90
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	157.630, 157.630, 157.537, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 18.3

The binding sites of Magnesium atom in the D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate (pdb code 4pb5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate, PDB code: 4pb5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:31.2 occ:1.00 OD2 A:BH2403 2.0 30.0 1.0 O A:HOH666 2.0 24.4 1.0 O A:HOH699 2.1 26.8 1.0 O A:HOH630 2.1 25.1 1.0 OB A:BH2403 2.3 22.6 1.0 CG A:BH2403 2.8 30.9 1.0 CB A:BH2403 3.0 27.9 1.0 SG A:CYS353 3.5 21.6 1.0 O A:HOH654 3.5 22.1 1.0 OH A:TYR177 3.8 26.5 1.0 NZ A:LYS43 3.9 25.4 1.0 O A:BH2403 3.9 27.2 1.0 OD1 A:BH2403 4.0 29.9 1.0 O3P A:PLP401 4.0 18.9 1.0 O A:HOH710 4.1 31.7 1.0 CB A:CYS353 4.1 13.1 1.0 CA A:BH2403 4.1 25.6 1.0 O A:HOH663 4.3 25.1 1.0 O A:HOH600 4.3 20.8 1.0 OE1 B:GLN319 4.3 16.4 1.0 O A:HOH617 4.3 26.2 1.0 C A:BH2403 4.3 23.4 1.0 CE2 A:TYR177 4.4 27.3 1.0 CZ A:TYR177 4.4 27.0 1.0 O A:HOH612 4.5 25.9 1.0 O A:HOH644 4.9 20.3 1.0 CZ2 B:TRP280 4.9 15.9 1.0 N A:BH2403 4.9 23.6 1.0

Magnesium binding site 2 out of 2 in the D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of D-Threo-3-Hydroxyaspartate Dehydratase H351A Mutant Complexed with L- Erythro-3-Hydroxyaspartate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:29.7 occ:1.00 O B:HOH659 1.9 24.6 1.0 OD1 B:BH2403 2.0 31.8 1.0 O B:HOH660 2.0 28.6 1.0 O B:HOH658 2.2 26.4 1.0 OB B:BH2403 2.3 24.1 1.0 CG B:BH2403 2.9 33.3 1.0 CB B:BH2403 3.1 27.3 1.0 SG B:CYS353 3.5 21.1 1.0 O B:HOH627 3.6 20.0 1.0 OXT B:BH2403 3.7 23.2 1.0 NZ B:LYS43 3.8 21.9 1.0 CB B:CYS353 4.0 15.8 1.0 OD2 B:BH2403 4.0 28.9 1.0 O1P B:PLP401 4.1 17.9 1.0 OH B:TYR177 4.1 28.1 1.0 CA B:BH2403 4.1 23.9 1.0 OE1 A:GLN319 4.2 14.6 1.0 O B:HOH661 4.2 25.0 1.0 O B:HOH655 4.3 35.9 1.0 C B:BH2403 4.3 20.6 1.0 O B:HOH657 4.4 19.5 1.0 O B:HOH600 4.4 18.4 1.0 CE2 B:TYR177 4.5 26.7 1.0 O B:HOH596 4.6 24.9 1.0 CZ B:TYR177 4.6 28.2 1.0 CZ2 A:TRP280 4.8 14.9 1.0 N B:BH2403 4.9 22.6 1.0 O B:HOH620 5.0 19.6 1.0

Y.Matsumoto, Y.Yasutake, Y.Takeda, T.Tamura, A.Yokota, M.Wada. Structure of D-Threo-3-Hydroxyaspartate Dehydratase To Be Published.