Magnesium in PDB 1kkr: Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid

All present enzymatic activity of Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid:
4.3.1.2;

The structure of Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid, PDB code: 1kkr was solved by C.W.Levy, P.A.Buckley, S.Sedelnikova, K.Kato, Y.Asano, D.W.Rice, P.J.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.00 / 2.10
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	129.537, 238.933, 66.269, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 22.3

The binding sites of Magnesium atom in the Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid (pdb code 1kkr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid, PDB code: 1kkr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic 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 Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:26.3 occ:1.00 OD2 A:ASP238 2.1 21.8 1.0 O A:HOH1124 2.1 27.7 1.0 O A:HOH1070 2.1 20.6 1.0 OD2 A:ASP307 2.2 24.7 1.0 OD1 A:2AS801 2.2 23.0 1.0 OE2 A:GLU273 2.2 25.3 1.0 CD A:GLU273 3.1 24.4 1.0 CG A:2AS801 3.1 26.2 1.0 CG A:ASP238 3.1 21.8 1.0 CG A:ASP307 3.2 24.3 1.0 OD2 A:2AS801 3.3 26.7 1.0 OD1 A:ASP238 3.5 20.0 1.0 CB A:ASP307 3.7 25.1 1.0 CG A:GLU273 3.7 23.4 1.0 NE2 A:GLN329 3.8 25.5 1.0 OE1 A:GLU273 3.9 26.3 1.0 O A:HOH824 4.1 21.7 1.0 OE1 A:GLU308 4.1 29.8 1.0 O A:HOH853 4.2 21.4 1.0 NZ A:LYS331 4.2 18.8 1.0 OD1 A:ASP307 4.3 24.4 1.0 OE2 A:GLU308 4.3 30.3 1.0 CB A:ASP238 4.4 23.1 1.0 NE2 A:HIS194 4.4 18.5 1.0 CB A:2AS801 4.5 26.4 1.0 CD A:GLU308 4.6 29.3 1.0 O A:HOH882 4.9 25.2 1.0 CB A:GLU273 4.9 21.9 1.0 CE A:LYS331 5.0 23.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:25.3 occ:1.00 O B:HOH527 2.1 21.6 1.0 OD2 B:ASP307 2.1 27.5 1.0 OD2 B:ASP238 2.1 24.9 1.0 O B:HOH536 2.1 23.8 1.0 OE2 B:GLU273 2.2 24.9 1.0 OD1 A:2AS800 2.2 29.1 1.0 CG A:2AS800 3.0 30.2 1.0 CG B:ASP307 3.1 25.9 1.0 OD2 A:2AS800 3.1 28.2 1.0 CG B:ASP238 3.1 24.2 1.0 CD B:GLU273 3.1 26.4 1.0 OD1 B:ASP238 3.5 22.7 1.0 CB B:ASP307 3.7 24.2 1.0 CG B:GLU273 3.8 23.2 1.0 NE2 B:GLN329 3.8 20.7 1.0 OE1 B:GLU308 3.9 36.3 1.0 OE1 B:GLU273 4.0 23.4 1.0 NZ B:LYS331 4.0 24.6 1.0 O B:HOH508 4.1 16.3 1.0 OD1 B:ASP307 4.2 23.8 1.0 OE2 B:GLU308 4.3 33.4 1.0 CB B:ASP238 4.4 23.0 1.0 CB A:2AS800 4.5 28.0 1.0 NE2 B:HIS194 4.5 19.4 1.0 O B:HOH565 4.5 27.9 1.0 CD B:GLU308 4.5 34.3 1.0 CE1 B:TYR240 4.8 47.3 1.0 CE B:LYS331 4.9 29.3 1.0

C.W.Levy, P.A.Buckley, S.Sedelnikova, Y.Kato, Y.Asano, D.W.Rice, P.J.Baker. Insights Into Enzyme Evolution Revealed By the Structure of Methylaspartate Ammonia Lyase. Structure V. 10 105 2002.
ISSN: ISSN 0969-2126
PubMed: 11796115
DOI: 10.1016/S0969-2126(01)00696-7