Sodium in PDB 8rj0: Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation

All present enzymatic activity of Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation:
4.3.1.1;

The structure of Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation, PDB code: 8rj0 was solved by N.Capra, A.M.W.H.Thunnissen, D.B.Janssen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.57 / 1.90
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	75.866, 98.992, 136.451, 90, 90, 90
R / Rfree (%)	16.9 / 20.7

The binding sites of Sodium atom in the Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation (pdb code 8rj0). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation, PDB code: 8rj0:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:43.4 occ:0.50 O A:HOH657 2.3 35.6 1.0 O A:HOH634 2.4 30.2 1.0 OD1 A:ASN343 2.8 34.4 1.0 NE2 A:GLN339 3.4 32.4 1.0 OD1 A:ASN368 3.7 30.0 1.0 O A:HOH686 3.9 35.4 0.5 CG A:ASN343 4.0 31.5 1.0 CD A:GLN339 4.2 29.5 1.0 N A:ASN343 4.4 25.4 1.0 OE1 A:GLN371 4.5 37.0 1.0 OE1 A:GLN339 4.6 27.8 1.0 CA A:ASN343 4.6 26.6 1.0 O A:GLN339 4.8 27.5 1.0 C A:GLY342 4.8 26.7 1.0 ND2 A:ASN343 4.9 33.9 1.0 CG A:ASN368 4.9 31.8 1.0 CB A:ASN343 4.9 26.9 1.0 OG1 A:THR346 5.0 28.4 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Mutant Aspartase From Bacillus Sp. YM55-1 in the Closed Loop Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Na501 b:38.7 occ:0.50 O B:HOH642 2.2 29.1 1.0 O B:HOH626 2.6 27.7 1.0 OD1 B:ASN343 2.8 29.0 1.0 NE2 B:GLN339 3.6 27.6 1.0 OD1 B:ASN368 3.8 28.4 1.0 CG B:ASN343 4.0 26.9 1.0 CD B:GLN339 4.3 27.1 1.0 N B:ASN343 4.3 24.8 1.0 O B:HOH686 4.3 36.5 0.5 CA B:ASN343 4.5 23.5 1.0 C B:GLY342 4.6 25.9 1.0 OE1 B:GLN339 4.7 25.3 1.0 O B:GLN339 4.7 27.2 1.0 OE1 B:GLN371 4.7 33.0 1.0 O B:GLY342 4.9 25.0 1.0 CB B:ASN343 4.9 25.3 1.0 OG1 B:THR346 4.9 24.9 1.0 ND2 B:ASN343 4.9 28.3 1.0 CG B:ASN368 4.9 24.5 1.0

A.Gran-Scheuch, H.J.Wijma, N.Capra, H.L.Van Beek, M.Trajkovic, K.Baldenius, M.Breuer, A.M.W.H.Thunnissen, D.B.Janssen. Bioinformatics and Computationally Supported Redesign of Aspartase For Beta-Alanine Synthesis By Acrylic Acid Hydroamination Acs Catalysis 928 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C05525