Calcium in PDB 3r6y: Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1

All present enzymatic activity of Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1:
4.3.1.1;

The structure of Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1, PDB code: 3r6y 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)	40.00 / 3.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.310, 168.940, 149.080, 90.00, 92.23, 90.00
R / Rfree (%)	24 / 29.7

The binding sites of Calcium atom in the Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1 (pdb code 3r6y). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1, PDB code: 3r6y:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Chymotrypsin-Treated 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 Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca402 b:80.5 occ:1.00 OD1 C:ASN343 2.9 43.1 1.0 OD1 B:ASN343 3.1 42.0 1.0 OD1 B:ASN368 3.6 41.4 1.0 OE1 C:GLN339 3.7 45.2 1.0 OD1 C:ASN368 4.0 42.2 1.0 N C:ASN343 4.1 40.2 1.0 CG C:ASN343 4.1 41.1 1.0 N B:ASN343 4.2 40.7 1.0 CG B:ASN343 4.3 40.8 1.0 CD C:GLN339 4.3 44.1 1.0 C C:GLY342 4.3 40.2 1.0 NE2 C:GLN339 4.4 43.9 1.0 O C:GLN339 4.4 43.6 1.0 CA B:ASN343 4.4 40.4 1.0 NE2 B:GLN339 4.4 48.7 1.0 CA C:ASN343 4.5 40.3 1.0 C B:GLY342 4.6 40.9 1.0 OG1 B:THR346 4.6 37.9 1.0 CG B:ASN368 4.6 42.1 1.0 OE1 B:GLN339 4.7 50.7 1.0 O C:GLY342 4.7 40.2 1.0 CA C:GLY342 4.8 40.3 1.0 O B:GLN339 4.8 47.0 1.0 CD B:GLN339 4.9 48.9 1.0 CB C:ASN343 4.9 40.5 1.0 OE1 C:GLN371 5.0 39.7 1.0 ND2 C:ASN343 5.0 41.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Chymotrypsin-Treated 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 Crystal Structure of Chymotrypsin-Treated Aspartase From Bacillus Sp. YM55-1 within 5.0Å range: probe atom residue distance (Å) B Occ F:Ca402 b:87.2 occ:1.00 OD1 G:ASN343 2.9 43.1 1.0 OD1 F:ASN343 3.0 41.3 1.0 OE1 F:GLN339 3.5 50.3 1.0 NE2 F:GLN339 3.7 49.1 1.0 OD1 G:ASN368 3.7 43.1 1.0 CD F:GLN339 3.9 49.4 1.0 NE2 G:GLN339 3.9 42.3 1.0 CG F:ASN343 4.0 40.0 1.0 CG G:ASN343 4.1 41.4 1.0 OD1 F:ASN368 4.1 41.8 1.0 N F:ASN343 4.4 40.6 1.0 OE1 F:GLN371 4.4 43.6 1.0 CA G:ASN343 4.5 40.5 1.0 N G:ASN343 4.5 40.6 1.0 CA F:ASN343 4.6 40.2 1.0 ND2 F:ASN343 4.7 39.2 1.0 O F:GLN339 4.7 47.3 1.0 CG G:ASN368 4.7 42.9 1.0 C F:GLY342 4.7 41.3 1.0 OG1 G:THR346 4.8 39.8 1.0 CD G:GLN339 4.8 43.5 1.0 OE1 G:GLN371 4.9 40.4 1.0 C G:GLY342 4.9 40.6 1.0 CB G:ASN343 4.9 40.7 1.0 OE1 G:GLN339 4.9 44.3 1.0 CB F:ASN343 4.9 40.3 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