Calcium in PDB 1w4y: Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide

All present enzymatic activity of Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide:
1.11.1.7;

The structure of Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide, PDB code: 1w4y was solved by G.H.Carlsson, P.Nicholls, D.Svistunenko, G.I.Berglund, J.Hajdu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.94 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.430, 67.563, 117.192, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 21.1

The structure of Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide (pdb code 1w4y). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide, PDB code: 1w4y:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1308 b:9.2 occ:1.00 O A:VAL46 2.4 11.6 1.0 O A:ASP43 2.5 10.6 1.0 OD1 A:ASP50 2.5 10.0 1.0 OD1 A:ASP43 2.5 10.7 1.0 O A:GLY48 2.6 11.0 1.0 O A:HOH2095 2.6 10.2 1.0 OG A:SER52 2.6 11.4 1.0 C A:ASP43 3.3 9.6 1.0 CG A:ASP50 3.5 9.7 1.0 C A:VAL46 3.5 9.6 1.0 CG A:ASP43 3.6 11.2 1.0 CB A:SER52 3.7 11.1 1.0 CA A:ASP43 3.7 8.8 1.0 C A:GLY48 3.8 8.9 1.0 N A:SER52 3.9 10.1 1.0 OD2 A:ASP50 4.0 10.1 1.0 N A:ASP50 4.0 9.8 1.0 CB A:VAL46 4.2 9.5 1.0 CA A:VAL46 4.2 10.0 1.0 CB A:ASP43 4.3 10.2 1.0 CA A:SER52 4.3 9.6 1.0 N A:GLY48 4.3 8.6 1.0 N A:VAL46 4.4 9.4 1.0 N A:CYS44 4.4 9.3 1.0 C A:ASN47 4.5 9.6 1.0 N A:ILE53 4.5 10.9 1.0 OD2 A:ASP43 4.5 10.5 1.0 N A:ASN47 4.6 9.4 1.0 N A:ALA51 4.6 10.3 1.0 OE1 A:GLU64 4.6 9.3 1.0 CA A:CYS49 4.6 9.5 1.0 N A:CYS49 4.7 8.6 1.0 CB A:ASP50 4.7 10.1 1.0 CA A:GLY48 4.7 8.2 1.0 CB A:ASN47 4.7 10.8 1.0 CA A:ASP50 4.7 10.7 1.0 O A:HIS42 4.7 10.5 1.0 OE2 A:GLU64 4.8 10.1 1.0 CA A:ASN47 4.8 10.7 1.0 C A:ASP50 4.8 10.8 1.0 O A:ASN47 4.8 10.7 1.0 C A:SER52 4.8 9.8 1.0 CA A:CYS44 4.8 9.4 1.0 C A:CYS49 4.8 10.9 1.0 CG1 A:VAL46 4.9 12.1 1.0 C A:ALA51 5.0 10.9 1.0

Calcium binding site 2 out of 2 in the Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ferrous Horseradish Peroxidase C1A in Complex with Carbon Monoxide within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1309 b:12.7 occ:1.00 O A:THR171 2.4 12.0 1.0 OG1 A:THR225 2.5 15.1 1.0 O A:ILE228 2.5 14.8 1.0 OD2 A:ASP222 2.6 16.8 1.0 O A:THR225 2.6 15.2 1.0 OG1 A:THR171 2.7 14.9 1.0 OD1 A:ASP230 2.7 17.6 1.0 C A:THR171 3.4 12.8 1.0 CG A:ASP230 3.5 17.0 1.0 CG A:ASP222 3.5 12.6 1.0 C A:THR225 3.6 14.4 1.0 CB A:THR225 3.6 15.2 1.0 C A:ILE228 3.7 16.5 1.0 OD2 A:ASP230 3.7 17.1 1.0 CB A:THR171 3.7 13.0 1.0 CA A:THR171 3.9 13.2 1.0 CB A:ASP222 4.0 13.1 1.0 CA A:THR225 4.0 14.9 1.0 N A:ASP230 4.1 15.8 1.0 CG2 A:THR171 4.2 13.2 1.0 N A:THR225 4.3 15.2 1.0 CB A:LYS232 4.3 15.1 1.0 N A:ILE228 4.4 16.6 1.0 CA A:ILE228 4.4 16.3 1.0 O A:ASP230 4.5 14.9 1.0 OD1 A:ASP222 4.6 15.3 1.0 CB A:ILE228 4.6 18.0 1.0 N A:PHE172 4.6 13.7 1.0 CB A:ASP230 4.7 15.8 1.0 N A:PHE229 4.7 14.8 1.0 N A:PRO226 4.7 14.8 1.0 CG A:LYS232 4.7 17.8 1.0 CA A:PHE229 4.8 15.4 1.0 CA A:ASP230 4.8 15.3 1.0 C A:ASP230 4.9 15.5 1.0 CG2 A:THR225 4.9 16.6 1.0 C A:PHE229 4.9 15.5 1.0 CA A:PHE172 5.0 13.4 1.0

G.H.Carlsson, P.Nicholls, D.Svistunenko, G.I.Berglund, J.Hajdu. Complexes of Horseradish Peroxidase with Formate, Acetate, and Carbon Monoxide Biochemistry V. 44 635 2005.
ISSN: ISSN 0006-2960
PubMed: 15641789
DOI: 10.1021/BI0483211