Magnesium in PDB 3zvh: Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A

All present enzymatic activity of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A:
4.3.1.2;

The structure of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A, PDB code: 3zvh was solved by H.Raj, W.Szymanski, J.De Villiers, H.J.Rozeboom, V.P.Veetil, C.R.Reis, M.Devilliers, S.De Wildeman, F.J.Dekker, W.J.Quax, A.M.W.H.Thunnissen, B.L.Feringa, D.B.Janssen, G.J.Poelarends, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	77.71 / 1.99
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.788, 109.705, 110.096, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24.9

The structure of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A (pdb code 3zvh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A, PDB code: 3zvh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1421 b:14.4 occ:1.00 OD2 A:ASP307 2.0 11.2 1.0 OE2 A:GLU273 2.0 20.7 1.0 OD2 A:ASP238 2.1 16.4 1.0 O A:HOH2182 2.2 12.8 1.0 O A:HOH2181 2.2 9.3 1.0 O A:HOH2180 2.3 13.6 1.0 CG A:ASP238 3.0 16.5 1.0 CD A:GLU273 3.1 20.2 1.0 CG A:ASP307 3.1 12.2 1.0 OD1 A:ASP238 3.3 18.4 1.0 CB A:ASP307 3.6 12.5 1.0 CG A:GLU273 3.8 16.9 1.0 NE2 A:GLN329 3.9 16.2 1.0 OE1 A:GLU273 4.0 20.8 1.0 OE2 A:GLU308 4.0 13.2 1.0 O A:HOH2160 4.1 9.1 1.0 OD1 A:ASP307 4.2 11.7 1.0 OE1 A:GLU308 4.3 15.8 1.0 CB A:ASP238 4.3 16.0 1.0 O A:HOH2082 4.5 23.6 1.0 CD A:GLU308 4.6 16.1 1.0 O A:HOH2214 4.6 21.6 1.0 NE2 A:HIS194 4.7 13.4 1.0 O A:HOH2183 4.7 24.3 1.0 CB A:GLU273 4.8 14.8 1.0 CZ A:TYR240 4.8 22.5 1.0

Magnesium binding site 2 out of 2 in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1421 b:8.0 occ:1.00 OE2 B:GLU273 1.9 11.5 1.0 OD2 B:ASP238 2.0 10.3 1.0 OD2 B:ASP307 2.0 12.3 1.0 O B:HOH2183 2.0 3.0 1.0 O B:HOH2184 2.1 13.2 1.0 O B:HOH2182 2.2 2.0 1.0 CG B:ASP238 2.9 12.3 1.0 CD B:GLU273 3.1 13.1 1.0 CG B:ASP307 3.1 11.4 1.0 OD1 B:ASP238 3.2 12.9 1.0 CB B:ASP307 3.7 9.7 1.0 CG B:GLU273 3.7 10.6 1.0 OE1 B:GLU273 4.1 15.7 1.0 OE2 B:GLU308 4.1 14.6 1.0 OD1 B:ASP307 4.2 10.5 1.0 CB B:ASP238 4.2 12.1 1.0 OE1 B:GLU308 4.3 13.5 1.0 OE1 B:GLN329 4.3 13.6 1.0 NE2 B:HIS194 4.4 8.6 1.0 O B:HOH2138 4.5 6.7 1.0 CD B:GLU308 4.6 14.2 1.0 CE1 B:TYR240 4.7 17.1 1.0 O B:HOH2242 4.7 15.9 1.0 CB B:GLU273 4.7 9.2 1.0 CZ B:TYR240 4.7 16.1 1.0 OH B:TYR240 5.0 15.9 1.0

H.Raj, W.Szymanski, J.De Villiers, H.J.Rozeboom, V.P.Veetil, C.R.Reis, M.De Villiers, F.J.Dekker, S.De Wildeman, W.J.Quax, A.M.W.H.Thunnissen, B.L.Feringa, D.B.Janssen, G.J.Poelarends. Engineering Methylaspartate Ammonia Lyase For the Asymmetric Synthesis of Unnatural Amino Acids. Nat.Chem. V. 4 478 2012.
ISSN: ISSN 1755-4330
PubMed: 22614383
DOI: 10.1038/NCHEM.1338