Calcium in PDB 2eha: Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution

All present enzymatic activity of Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution:
1.11.1.7;

The structure of Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution, PDB code: 2eha was solved by A.K.Singh, A.S.Ethayathulla, N.Singh, S.Sharma, P.Kaur, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	57.991, 72.272, 83.652, 85.45, 84.04, 75.89
R / Rfree (%)	19.6 / 23.7

The structure of Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution (pdb code 2eha). 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 Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution, PDB code: 2eha:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution


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 Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca607 b:9.8 occ:1.00 O A:ASP110 2.5 10.4 1.0 O A:PHE186 2.6 14.9 1.0 OG1 A:THR184 2.6 11.5 1.0 OD1 A:ASP110 2.6 9.1 1.0 O A:THR184 2.7 10.6 1.0 OD1 A:ASP188 2.8 15.1 1.0 OG A:SER190 2.9 23.1 1.0 C A:THR184 3.3 12.0 1.0 CG A:ASP188 3.6 15.8 1.0 C A:ASP110 3.6 11.6 1.0 C A:PHE186 3.7 13.7 1.0 OD2 A:ASP188 3.8 16.5 1.0 CG A:ASP110 3.8 9.1 1.0 CB A:THR184 3.8 13.5 1.0 N A:PHE186 3.9 15.9 1.0 CB A:SER190 3.9 20.5 1.0 CA A:THR184 3.9 12.0 1.0 N A:SER185 4.1 14.5 1.0 N A:THR184 4.1 10.7 1.0 C A:SER185 4.2 16.2 1.0 N A:ASP188 4.2 13.7 1.0 CA A:SER185 4.4 16.6 1.0 CA A:PHE186 4.4 14.1 1.0 CA A:ASP110 4.4 11.6 1.0 N A:LEU111 4.5 10.8 1.0 OD2 A:ASP110 4.5 12.3 1.0 CA A:LEU111 4.5 9.2 1.0 CB A:ASP110 4.7 10.8 1.0 N A:LEU187 4.8 13.2 1.0 O A:SER185 4.8 17.6 1.0 CB A:ASP188 4.8 14.4 1.0 N A:SER190 4.8 19.6 1.0 CG2 A:THR184 4.9 15.1 1.0 CG2 A:VAL183 4.9 12.7 1.0 C A:VAL183 5.0 10.5 1.0 CA A:LEU187 5.0 13.1 1.0 CA A:ASP188 5.0 14.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution


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 Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca607 b:18.9 occ:1.00 O B:ASP110 2.5 10.6 1.0 O B:PHE186 2.6 10.6 1.0 OG1 B:THR184 2.6 9.7 1.0 OD1 B:ASP110 2.6 13.2 1.0 O B:THR184 2.7 11.2 1.0 OD1 B:ASP188 2.8 22.3 1.0 OG B:SER190 3.0 23.2 1.0 CB B:SER190 3.3 17.8 1.0 CG B:ASP188 3.5 20.6 1.0 C B:THR184 3.6 12.1 1.0 C B:ASP110 3.6 9.9 1.0 OD2 B:ASP188 3.7 22.4 1.0 CG B:ASP110 3.7 14.7 1.0 C B:PHE186 3.8 11.3 1.0 CB B:THR184 3.8 12.4 1.0 N B:ASP188 3.9 14.1 1.0 CA B:THR184 4.1 12.9 1.0 N B:SER190 4.1 13.4 1.0 N B:PHE186 4.2 12.0 1.0 N B:THR184 4.2 14.8 1.0 CA B:SER190 4.3 14.9 1.0 CA B:ASP110 4.3 11.4 1.0 OD2 B:ASP110 4.5 17.7 1.0 CA B:PHE186 4.6 11.6 1.0 CB B:ASP110 4.6 11.8 1.0 CB B:ASP188 4.6 16.0 1.0 CA B:ASP188 4.6 14.1 1.0 N B:LEU111 4.7 9.1 1.0 N B:SER185 4.7 12.1 1.0 N B:LEU187 4.8 12.6 1.0 N B:ALA189 4.8 11.4 1.0 CA B:LEU187 4.8 13.4 1.0 C B:SER185 4.8 11.8 1.0 CA B:LEU111 4.8 9.1 1.0 C B:LEU187 4.9 14.2 1.0 C B:ASP188 4.9 11.9 1.0 CG2 B:THR184 4.9 13.2 1.0

A.K.Singh, A.S.Ethayathulla, N.Singh, S.Sharma, A.Bhushan, P.Kaur, T.P.Singh. Crystal Structure of Goat Lactoperoxidase Complexed with Formate Anion at 3.3 A Resolution To Be Published.