Calcium in PDB 5ffn: Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A

All present enzymatic activity of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A:
3.4.21.14;

The structure of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A, PDB code: 5ffn was solved by K.E.Mcauley, A.Svendsen, P.R.Oestergaard, J.Dohnalek, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.753, 66.838, 107.082, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 18.8

The structure of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Calcium atom in the Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A (pdb code 5ffn). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A, PDB code: 5ffn:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:13.8 occ:1.00 O A:ILE220 2.2 12.9 1.0 O A:THR215 2.3 15.7 1.0 OD1 A:ASP218 2.3 17.9 1.0 O A:HOH546 2.3 11.1 1.0 OD2 A:ASP225 2.3 12.7 1.0 OE1 A:GLN222 2.4 21.5 1.0 CG A:ASP218 3.2 19.6 1.0 CG A:ASP225 3.3 11.4 1.0 OD2 A:ASP218 3.3 20.3 1.0 CD A:GLN222 3.4 20.6 1.0 C A:ILE220 3.4 13.7 1.0 C A:THR215 3.5 16.4 1.0 OD1 A:ASP225 3.8 11.8 1.0 NE2 A:GLN222 3.9 22.9 1.0 N A:GLN222 4.1 13.6 1.0 N A:ILE220 4.2 13.8 1.0 CB A:THR215 4.2 17.8 1.0 O A:HOH591 4.3 32.4 1.0 CA A:ILE220 4.3 15.3 1.0 N A:ILE221 4.4 14.6 1.0 CA A:ILE221 4.4 14.0 1.0 N A:ALA216 4.4 15.1 1.0 CA A:THR215 4.4 16.4 1.0 OD2 A:ASP299 4.4 14.2 1.0 CB A:ASP225 4.4 11.9 1.0 CA A:ALA216 4.4 16.5 1.0 CB A:ASP218 4.6 17.5 1.0 C A:ILE221 4.6 14.3 1.0 CG A:GLN222 4.6 18.5 1.0 OG1 A:THR215 4.7 14.7 1.0 CB A:GLN222 4.7 15.9 1.0 N A:ASP218 4.8 17.8 1.0 CB A:ILE220 4.8 16.0 1.0 O A:HOH596 4.8 10.3 1.0

Calcium binding site 2 out of 2 in the Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:18.9 occ:1.00 O A:GLY298 2.3 12.7 1.0 O A:GLY296 2.3 16.2 1.0 O A:ILE289 2.4 12.6 1.0 OD1 A:ASP288 2.4 17.3 1.0 O A:HOH559 2.4 11.9 1.0 OD2 A:ASP300 2.4 13.4 1.0 C A:GLY298 3.4 14.4 1.0 C A:ILE289 3.5 13.1 1.0 CG A:ASP300 3.5 12.4 1.0 C A:GLY296 3.5 17.1 1.0 CG A:ASP288 3.6 15.9 1.0 OG A:SER303 3.7 11.7 1.0 N A:GLY298 3.7 14.7 1.0 N A:ILE289 3.7 10.8 1.0 N A:GLY296 4.0 16.4 1.0 C A:THR297 4.1 16.0 1.0 OD2 A:ASP288 4.1 15.8 1.0 CA A:GLY298 4.1 14.4 1.0 CA A:ILE289 4.2 12.2 1.0 O A:HOH567 4.2 14.1 1.0 CB A:ASP300 4.2 13.2 1.0 O A:GLY304 4.4 10.2 1.0 CA A:THR297 4.4 16.4 1.0 CA A:GLY296 4.4 17.5 1.0 N A:THR297 4.4 16.8 1.0 N A:ASP300 4.4 13.2 1.0 OD1 A:ASP300 4.4 13.3 1.0 C A:ASP288 4.5 12.7 1.0 N A:LYS290 4.5 14.7 1.0 N A:ASP299 4.5 13.7 1.0 O A:THR297 4.7 17.6 1.0 CB A:ASP288 4.7 12.0 1.0 CA A:ASP288 4.8 11.9 1.0 CA A:LYS290 4.8 16.2 1.0 C A:ASP299 4.8 14.3 1.0 CB A:ILE289 4.8 11.8 1.0 CG A:LYS290 4.8 20.1 1.0 CA A:ASP299 4.8 13.8 1.0 CA A:ASP300 5.0 12.8 1.0

J.Dohnalek, K.E.Mcauley, A.M.Brzozowski, P.R.Oestergaard, A.Svendsen, K.S.Wilson. Stabilization of Enzymes By Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family To Be Published 203 2016.
DOI: 10.4032/9789814669337