Calcium in PDB 3csu: Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase

All present enzymatic activity of Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase:
2.1.3.2;

The structure of Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase, PDB code: 3csu was solved by P.T.Beernink, J.A.Endrizzi, T.Alber, H.K.Schachman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.120, 82.540, 210.520, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase (pdb code 3csu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase, PDB code: 3csu:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca311 b:16.4 occ:1.00 O B:HOH543 2.0 53.6 1.0 OD2 B:ASP153 2.1 27.0 1.0 O B:HOH484 2.5 22.7 1.0 CG B:ASP153 3.4 11.9 1.0 CB B:ASP153 4.2 9.4 1.0 O B:HOH362 4.2 18.5 1.0 OD1 B:ASP153 4.3 16.4 1.0 O B:HOH397 4.4 15.4 1.0 NH2 B:ARG17 4.6 37.2 1.0 OD2 B:ASP180 4.9 19.8 1.0

Calcium binding site 2 out of 2 in the Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Catalytic Trimer of Escherichia Coli Aspartate Transcarbamoylase within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca311 b:26.8 occ:1.00 O C:HOH398 2.2 17.5 1.0 O C:GLY120 2.2 24.8 1.0 O C:HOH507 2.3 30.6 1.0 O C:HOH320 2.5 13.8 1.0 C C:GLY120 3.2 12.9 1.0 CA C:GLY120 4.0 18.0 1.0 N C:ASN121 4.1 10.4 1.0 CA C:ASN121 4.2 10.9 1.0 N C:GLY120 4.3 21.1 1.0 CE1 C:HIS8 4.4 12.4 1.0 O C:HOH399 4.4 17.5 1.0 O C:THR116 4.5 15.9 1.0 O C:HOH401 4.7 16.2 1.0 O C:HOH328 4.8 24.1 1.0 NE2 C:HIS8 4.9 28.1 1.0 O C:HOH353 4.9 17.7 1.0 OG C:SER119 5.0 13.6 1.0

P.T.Beernink, J.A.Endrizzi, T.Alber, H.K.Schachman. Assessment of the Allosteric Mechanism of Aspartate Transcarbamoylase Based on the Crystalline Structure of the Unregulated Catalytic Subunit. Proc.Natl.Acad.Sci.Usa V. 96 5388 1999.
ISSN: ISSN 0027-8424
PubMed: 10318893
DOI: 10.1073/PNAS.96.10.5388