Calcium in PDB 3r6q: A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1

All present enzymatic activity of A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1:
4.3.1.1;

The structure of A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1, PDB code: 3r6q was solved by G.Fibriansah, V.Puthan Veetil, G.J.Poelarends, A.-M.W.H.Thunnissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.56 / 2.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	75.594, 118.194, 140.226, 89.85, 89.59, 76.51
R / Rfree (%)	19.9 / 25.3

The binding sites of Calcium atom in the A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1 (pdb code 3r6q). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1, PDB code: 3r6q:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca469 b:42.2 occ:1.00 OE1 A:GLU395 2.2 32.0 1.0 O A:ALA393 2.6 24.7 1.0 CD A:GLU395 3.3 31.8 1.0 C A:ALA393 3.8 24.4 1.0 OE2 A:GLU395 3.8 32.6 1.0 O A:HOH845 3.9 24.5 1.0 CA A:ASN394 4.4 25.5 1.0 N A:GLU395 4.5 27.4 1.0 CG A:GLU395 4.5 30.9 1.0 N A:ASN394 4.6 24.8 1.0 OD1 A:ASN394 4.7 23.0 1.0 N A:ALA393 4.8 23.3 1.0 CA A:ALA393 4.8 24.0 1.0

Calcium binding site 2 out of 4 in the A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca469 b:31.9 occ:1.00 OE1 D:GLU395 2.1 30.8 1.0 O D:ALA393 2.5 23.1 1.0 CD D:GLU395 3.2 31.4 1.0 OE2 D:GLU395 3.6 33.3 1.0 C D:ALA393 3.8 22.6 1.0 O D:HOH507 3.8 22.6 1.0 CG D:GLU395 4.4 28.9 1.0 CA D:ASN394 4.5 23.4 1.0 N D:GLU395 4.5 25.1 1.0 N D:ASN394 4.6 23.1 1.0 N D:ALA393 4.8 21.6 1.0 CA D:ALA393 4.8 22.1 1.0 O D:HOH529 4.8 22.4 1.0 OD1 D:ASN394 4.9 21.1 1.0

Calcium binding site 3 out of 4 in the A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1 within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca469 b:38.6 occ:1.00 OE2 E:GLU395 2.6 27.2 1.0 O E:ALA393 2.6 22.5 1.0 CD E:GLU395 3.4 26.2 1.0 OE1 E:GLU395 3.5 26.3 1.0 C E:ALA393 3.8 21.9 1.0 O E:HOH492 4.0 20.9 1.0 N E:GLU395 4.4 23.5 1.0 CA E:ASN394 4.4 22.3 1.0 N E:ASN394 4.5 22.0 1.0 OD1 E:ASN394 4.7 19.5 1.0 CG E:GLU395 4.8 24.8 1.0 CA E:ALA393 4.9 21.6 1.0 N E:ALA393 4.9 21.2 1.0 C E:ASN394 4.9 23.0 1.0

Calcium binding site 4 out of 4 in the A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of A Triclinic-Lattice Structure of Aspartase From Bacillus Sp. YM55-1 within 5.0Å range: probe atom residue distance (Å) B Occ H:Ca469 b:34.2 occ:1.00 O H:ALA393 2.5 22.0 1.0 OE1 H:GLU395 2.5 25.8 1.0 O H:HOH851 2.5 17.9 1.0 OD2 D:ASP67 2.6 32.1 1.0 CD H:GLU395 3.5 27.6 1.0 CG D:ASP67 3.5 30.4 1.0 C H:ALA393 3.7 21.5 1.0 OE2 H:GLU395 3.8 28.0 1.0 OD1 D:ASP67 3.8 30.7 1.0 N H:GLU395 4.2 24.6 1.0 CA H:ASN394 4.2 23.0 1.0 N H:ASN394 4.4 22.2 1.0 OE2 D:GLU69 4.5 32.6 1.0 C H:ASN394 4.8 23.7 1.0 OD1 H:ASN394 4.8 21.1 1.0 CA H:ALA393 4.8 20.7 1.0 N H:ALA393 4.8 20.0 1.0 CG H:GLU395 4.8 25.4 1.0 CB D:ASP67 4.9 29.8 1.0

G.Fibriansah, V.P.Veetil, G.J.Poelarends, A.M.Thunnissen. Structural Basis For the Catalytic Mechanism of Aspartate Ammonia Lyase. Biochemistry V. 50 6053 2011.
ISSN: ISSN 0006-2960
PubMed: 21661762
DOI: 10.1021/BI200497Y