Calcium in PDB 1h5a: Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate

All present enzymatic activity of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate:
1.11.1.7;

The structure of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate, PDB code: 1h5a was solved by G.I.Berglund, G.H.Carlsson, J.Hajdu, A.T.Smith, H.Szoke, A.Henriksen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.71 / 1.6
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.347, 67.774, 117.265, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 20.2

The structure of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate (pdb code 1h5a). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate, PDB code: 1h5a:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:9.1 occ:1.00 O A:VAL46 2.3 10.1 1.0 O A:ASP43 2.3 10.0 1.0 OD1 A:ASP43 2.3 8.9 1.0 OD1 A:ASP50 2.4 9.5 1.0 OG A:SER52 2.5 9.2 1.0 O A:HOH2118 2.5 8.1 1.0 O A:GLY48 2.5 9.7 1.0 C A:ASP43 3.2 10.1 1.0 CG A:ASP50 3.4 11.5 1.0 C A:VAL46 3.5 9.0 1.0 CG A:ASP43 3.5 11.2 1.0 CB A:SER52 3.6 10.0 1.0 CA A:ASP43 3.7 9.1 1.0 C A:GLY48 3.7 9.6 1.0 N A:SER52 3.9 10.3 1.0 N A:ASP50 4.0 9.5 1.0 OD2 A:ASP50 4.0 10.1 1.0 CB A:ASP43 4.2 9.6 1.0 CB A:VAL46 4.2 7.8 1.0 CA A:VAL46 4.2 9.2 1.0 CA A:SER52 4.3 10.5 1.0 N A:GLY48 4.3 9.6 1.0 N A:CYS44 4.4 9.6 1.0 N A:VAL46 4.4 8.5 1.0 C A:ASN47 4.4 10.4 1.0 OD2 A:ASP43 4.4 11.2 1.0 N A:ILE53 4.5 10.2 1.0 N A:ASN47 4.5 9.5 1.0 N A:ALA51 4.6 9.6 1.0 CA A:CYS49 4.6 8.9 1.0 CB A:ASP50 4.6 9.5 1.0 N A:CYS49 4.6 9.1 1.0 CA A:GLY48 4.6 9.1 1.0 CB A:ASN47 4.7 11.6 1.0 CA A:ASP50 4.7 9.6 1.0 OE1 A:GLU64 4.7 9.0 1.0 OE2 A:GLU64 4.7 9.7 1.0 O A:HIS42 4.7 10.3 1.0 CA A:ASN47 4.8 10.3 1.0 C A:ASP50 4.8 10.6 1.0 O A:ASN47 4.8 10.6 1.0 C A:CYS49 4.8 10.3 1.0 C A:SER52 4.8 10.3 1.0 CA A:CYS44 4.9 8.9 1.0 CG1 A:VAL46 4.9 10.7 1.0 C A:ALA51 5.0 11.1 1.0 N A:ASP43 5.0 9.7 1.0

Calcium binding site 2 out of 2 in the Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Ferric Horseradish Peroxidase C1A in Complex with Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:13.6 occ:1.00 OD2 A:ASP222 2.3 15.1 1.0 O A:THR171 2.3 11.9 1.0 OG1 A:THR225 2.4 13.6 1.0 O A:ILE228 2.4 13.7 1.0 O A:THR225 2.5 16.4 1.0 OG1 A:THR171 2.5 12.8 1.0 OD1 A:ASP230 2.6 16.4 1.0 C A:THR171 3.3 13.0 1.0 CG A:ASP222 3.4 11.6 1.0 CG A:ASP230 3.5 16.9 1.0 C A:THR225 3.5 14.1 1.0 CB A:THR225 3.5 13.8 1.0 C A:ILE228 3.6 15.2 1.0 CB A:THR171 3.6 12.1 1.0 CA A:THR171 3.8 11.6 1.0 OD2 A:ASP230 3.8 16.9 1.0 CB A:ASP222 3.9 11.4 1.0 CA A:THR225 4.0 13.7 1.0 N A:ASP230 4.2 16.0 1.0 CG2 A:THR171 4.2 11.8 1.0 N A:ILE228 4.3 15.8 1.0 N A:THR225 4.3 13.0 1.0 CA A:ILE228 4.4 15.8 1.0 OD1 A:ASP222 4.4 13.2 1.0 CB A:LYS232 4.5 15.7 1.0 N A:PHE172 4.5 13.6 1.0 CB A:ILE228 4.6 17.6 1.0 O A:ASP230 4.6 15.6 1.0 N A:PHE229 4.6 14.1 1.0 N A:PRO226 4.6 14.6 1.0 CB A:ASP230 4.7 16.2 1.0 CA A:PHE229 4.7 14.6 1.0 CG2 A:THR225 4.8 15.2 1.0 CG A:LYS232 4.9 20.0 1.0 CA A:ASP230 4.9 15.2 1.0 C A:PHE229 4.9 15.6 1.0 CA A:PHE172 4.9 12.6 1.0 C A:ASP230 5.0 15.9 1.0

G.I.Berglund, G.H.Carlsson, A.T.Smith, H.Szoke, A.Henriksen, J.Hajdu. The Catalytic Pathway of Horseradish Peroxidase at High Resolution Nature V. 417 463 2002.
ISSN: ISSN 0028-0836
PubMed: 12024218
DOI: 10.1038/417463A