Calcium in PDB 1kdq: Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin

All present enzymatic activity of Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin:
3.4.21.1;

The structure of Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin, PDB code: 1kdq was solved by E.Szabo, Z.Bocskei, G.Naray-Szabo, L.Graf, I.Venekei, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.97 / 2.55
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	74.589, 76.707, 83.478, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 27.7

The binding sites of Calcium atom in the Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin (pdb code 1kdq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin, PDB code: 1kdq:

Calcium binding site 1 out of 1 in the Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure Analysis of the Mutant S189D Rat Chymotrypsin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca246 b:48.3 occ:1.00 OE2 A:GLU78 2.3 53.1 1.0 OE1 A:GLU70 2.3 38.7 1.0 O A:SER75 2.6 80.9 1.0 O A:ASP72 2.8 26.8 1.0 O A:ASP76 2.8 90.9 1.0 OE2 A:GLU70 2.9 38.7 1.0 O A:HOH316 3.0 38.9 1.0 CD A:GLU70 3.0 38.7 1.0 CD A:GLU78 3.4 53.1 1.0 C A:SER75 3.8 80.9 1.0 CG A:GLU78 3.8 53.1 1.0 C A:ASP76 3.9 90.9 1.0 C A:ASP72 3.9 26.8 1.0 OE1 A:GLU78 4.4 53.1 1.0 N A:GLU78 4.4 58.5 1.0 CG A:GLU70 4.4 38.7 1.0 CB A:ASP76 4.6 90.9 1.0 CA A:ASP76 4.6 90.9 1.0 CA A:GLN73 4.6 30.3 1.0 N A:GLN73 4.7 30.3 1.0 N A:ASP76 4.7 90.9 1.0 O A:HOH303 4.7 22.0 1.0 N A:GLU77 4.7 72.6 1.0 N A:ASP72 4.8 26.8 1.0 CA A:SER75 4.8 80.9 1.0 CA A:GLU77 4.8 72.6 1.0 CA A:ASP72 4.8 26.8 1.0 CG2 A:ILE80 4.9 46.7 1.0 C A:GLN73 4.9 30.3 1.0 O A:GLU78 4.9 58.5 1.0 CB A:GLU78 5.0 58.5 1.0

E.Szabo, I.Venekei, Z.Bocskei, G.Naray-Szabo, L.Graf. Three Dimensional Structures of S189D Chymotrypsin and D189S Trypsin Mutants: the Effect of Polarity at Site 189 on A Protease-Specific Stabilization of the Substrate-Binding Site J.Mol.Biol. V. 331 1121 2003.
ISSN: ISSN 0022-2836
PubMed: 12927546
DOI: 10.1016/S0022-2836(03)00849-0