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

Enzymatic activity of 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;

Protein crystallography data

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

Calcium Binding Sites:

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 3r6y

Go back to Calcium Binding Sites List in 3r6y
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 3r6y

Go back to Calcium Binding Sites List in 3r6y
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

Reference:

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
Page generated: Tue Jul 8 16:13:11 2025

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