Calcium in PDB 7atj: Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid

All present enzymatic activity of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid:
1.11.1.7;

The structure of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid, PDB code: 7atj was solved by A.Henriksen, A.T.Smith, M.Gajhede, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.00 / 1.47
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.868, 66.930, 119.017, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 20.3

The structure of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid (pdb code 7atj). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid, PDB code: 7atj:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:8.3 occ:1.00 O A:VAL46 2.3 7.4 1.0 OD1 A:ASP50 2.3 9.4 1.0 OD1 A:ASP43 2.4 8.4 1.0 O A:ASP43 2.4 9.1 1.0 O A:HOH1001 2.4 7.2 1.0 OG A:SER52 2.5 9.1 1.0 O A:GLY48 2.5 8.5 1.0 C A:ASP43 3.3 9.0 1.0 CG A:ASP50 3.4 10.0 1.0 C A:VAL46 3.5 7.9 1.0 CG A:ASP43 3.6 10.8 1.0 CB A:SER52 3.6 6.6 1.0 CA A:ASP43 3.7 8.0 1.0 C A:GLY48 3.7 8.2 1.0 N A:SER52 3.8 10.1 1.0 OD2 A:ASP50 4.0 9.8 1.0 N A:ASP50 4.1 8.9 1.0 CA A:SER52 4.2 10.0 1.0 CA A:VAL46 4.2 7.3 1.0 CB A:VAL46 4.2 7.3 1.0 CB A:ASP43 4.3 7.6 1.0 N A:GLY48 4.3 7.8 1.0 N A:VAL46 4.4 7.6 1.0 C A:ASN47 4.4 10.7 1.0 N A:CYS44 4.4 8.3 1.0 N A:ILE53 4.5 8.8 1.0 N A:ASN47 4.5 9.1 1.0 OD2 A:ASP43 4.6 9.0 1.0 N A:ALA51 4.6 9.1 1.0 CB A:ASP50 4.6 8.6 1.0 CA A:GLY48 4.6 8.1 1.0 N A:CYS49 4.7 9.1 1.0 CA A:ASP50 4.7 9.0 1.0 CB A:ASN47 4.7 11.7 1.0 CA A:CYS49 4.7 8.5 1.0 O A:HIS42 4.7 8.6 1.0 OE1 A:GLU64 4.7 7.7 1.0 CA A:ASN47 4.7 9.1 1.0 C A:ASP50 4.8 10.7 1.0 OE2 A:GLU64 4.8 9.0 1.0 C A:SER52 4.8 8.1 1.0 O A:ASN47 4.8 11.3 1.0 CG1 A:VAL46 4.9 13.6 1.0 C A:ALA51 4.9 8.1 1.0 CA A:CYS44 4.9 6.9 1.0 C A:CYS49 4.9 10.2 1.0 N A:ASP43 5.0 7.8 1.0

Calcium binding site 2 out of 2 in the Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Recombinant Horseradish Peroxidase C1A Complex with Cyanide and Ferulic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:10.3 occ:1.00 OD2 A:ASP222 2.2 12.6 1.0 O A:THR171 2.3 8.9 1.0 O A:ILE228 2.4 10.0 1.0 OG1 A:THR225 2.5 12.0 1.0 O A:THR225 2.5 12.3 1.0 OG1 A:THR171 2.5 11.0 1.0 OD1 A:ASP230 2.6 12.0 1.0 CG A:ASP222 3.4 10.6 1.0 C A:THR171 3.4 13.8 1.0 CG A:ASP230 3.5 17.3 1.0 C A:THR225 3.5 12.4 1.0 CB A:THR225 3.6 13.7 1.0 C A:ILE228 3.6 11.8 1.0 CB A:THR171 3.7 10.2 1.0 OD2 A:ASP230 3.8 12.4 1.0 CA A:THR171 3.9 9.7 1.0 CA A:THR225 4.0 10.1 1.0 CB A:ASP222 4.0 8.1 1.0 N A:ASP230 4.2 11.7 1.0 CG2 A:THR171 4.3 10.8 1.0 N A:THR225 4.3 11.2 1.0 N A:ILE228 4.3 11.8 1.0 CA A:ILE228 4.4 10.9 1.0 OD1 A:ASP222 4.4 10.1 1.0 N A:PHE172 4.6 12.0 1.0 CB A:LYS232 4.6 12.7 1.0 N A:PHE229 4.6 10.8 1.0 CB A:ILE228 4.6 15.5 1.0 O A:ASP230 4.6 12.2 1.0 N A:PRO226 4.7 11.4 1.0 CB A:ASP230 4.7 12.0 1.0 CA A:PHE229 4.8 9.4 1.0 CG2 A:THR225 4.9 12.4 1.0 CA A:ASP230 4.9 11.5 1.0 C A:PHE229 5.0 9.5 1.0

A.Henriksen, A.T.Smith, M.Gajhede. The Structures of the Horseradish Peroxidase C-Ferulic Acid Complex and the Ternary Complex with Cyanide Suggest How Peroxidases Oxidize Small Phenolic Substrates. J.Biol.Chem. V. 274 35005 1999.
ISSN: ISSN 0021-9258
PubMed: 10574977
DOI: 10.1074/JBC.274.49.35005