Calcium in PDB 6atj: Recombinant Horseradish Peroxidase C Complex with Ferulic Acid

All present enzymatic activity of Recombinant Horseradish Peroxidase C Complex with Ferulic Acid:
1.11.1.7;

The structure of Recombinant Horseradish Peroxidase C Complex with Ferulic Acid, PDB code: 6atj 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)	29.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.297, 67.272, 117.646, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 19.9

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

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Recombinant Horseradish Peroxidase C Complex with Ferulic Acid (pdb code 6atj). 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 C Complex with Ferulic Acid, PDB code: 6atj:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Recombinant Horseradish Peroxidase C Complex with 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 C Complex with Ferulic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:8.0 occ:1.00 OD1 A:ASP50 2.3 4.9 1.0 O A:ASP43 2.3 6.0 1.0 O A:VAL46 2.4 6.3 1.0 OD1 A:ASP43 2.4 4.0 1.0 OG A:SER52 2.5 5.3 1.0 O A:HOH1016 2.6 2.0 1.0 O A:GLY48 2.6 6.8 1.0 C A:ASP43 3.2 6.3 1.0 CG A:ASP50 3.4 6.9 1.0 C A:VAL46 3.5 6.8 1.0 CG A:ASP43 3.5 10.9 1.0 CB A:SER52 3.6 3.9 1.0 CA A:ASP43 3.6 6.7 1.0 C A:GLY48 3.8 7.2 1.0 N A:SER52 3.9 6.8 1.0 OD2 A:ASP50 3.9 4.2 1.0 N A:ASP50 4.0 6.6 1.0 CB A:ASP43 4.2 6.8 1.0 CB A:VAL46 4.2 7.0 1.0 CA A:SER52 4.3 6.6 1.0 CA A:VAL46 4.3 6.4 1.0 N A:CYS44 4.3 6.3 1.0 N A:ILE53 4.3 6.3 1.0 N A:GLY48 4.4 8.2 1.0 N A:VAL46 4.4 6.0 1.0 C A:ASN47 4.4 8.1 1.0 OD2 A:ASP43 4.5 6.6 1.0 N A:ALA51 4.5 7.0 1.0 N A:ASN47 4.6 7.1 1.0 OE1 A:GLU64 4.6 4.8 1.0 OE2 A:GLU64 4.6 7.2 1.0 CB A:ASP50 4.6 7.8 1.0 O A:HIS42 4.7 7.0 1.0 CA A:ASP50 4.7 7.0 1.0 CA A:GLY48 4.7 7.5 1.0 CA A:CYS49 4.7 7.0 1.0 CB A:ASN47 4.7 7.5 1.0 O A:ASN47 4.7 8.7 1.0 N A:CYS49 4.7 7.0 1.0 C A:SER52 4.8 6.5 1.0 C A:ASP50 4.8 7.0 1.0 CA A:ASN47 4.8 7.9 1.0 CA A:CYS44 4.8 6.0 1.0 N A:ASP43 4.9 6.4 1.0 C A:CYS49 4.9 7.0 1.0 C A:ALA51 4.9 6.8 1.0 CG1 A:VAL46 5.0 6.0 1.0

Calcium binding site 2 out of 2 in the Recombinant Horseradish Peroxidase C Complex with 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 C Complex with Ferulic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:10.3 occ:1.00 OD2 A:ASP222 2.3 9.1 1.0 O A:THR171 2.4 8.8 1.0 O A:ILE228 2.4 7.3 1.0 OD1 A:ASP230 2.4 7.6 1.0 OG1 A:THR225 2.5 6.6 1.0 O A:THR225 2.5 7.0 1.0 OG1 A:THR171 2.7 8.6 1.0 CG A:ASP230 3.4 10.9 1.0 CG A:ASP222 3.4 9.4 1.0 C A:THR225 3.4 7.6 1.0 C A:THR171 3.4 8.2 1.0 CB A:THR225 3.5 7.4 1.0 C A:ILE228 3.6 7.7 1.0 OD2 A:ASP230 3.7 8.6 1.0 CB A:THR171 3.8 7.8 1.0 CA A:THR225 3.9 7.5 1.0 CB A:ASP222 3.9 7.1 1.0 CA A:THR171 3.9 7.8 1.0 N A:ASP230 4.1 8.7 1.0 N A:THR225 4.2 7.4 1.0 N A:ILE228 4.2 8.2 1.0 CA A:ILE228 4.3 8.2 1.0 CG2 A:THR171 4.4 4.3 1.0 CB A:ILE228 4.4 8.3 1.0 OD1 A:ASP222 4.5 6.6 1.0 CB A:LYS232 4.6 6.9 0.5 N A:PRO226 4.6 8.1 1.0 N A:PHE172 4.6 8.1 1.0 CG A:LYS232 4.6 9.4 0.5 CB A:LYS232 4.6 5.8 0.5 CB A:ASP230 4.6 9.4 1.0 O A:ASP230 4.6 8.2 1.0 N A:PHE229 4.6 7.6 1.0 CA A:PHE229 4.8 8.1 1.0 CG2 A:THR225 4.8 8.0 1.0 CA A:ASP230 4.8 8.7 1.0 C A:PHE229 4.9 8.4 1.0 C A:ASP230 4.9 8.6 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