Calcium in PDB 1kzm: Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).

All present enzymatic activity of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).:
1.11.1.7;

The structure of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C)., PDB code: 1kzm was solved by K.Meno, 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)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.400, 66.700, 117.100, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 20.3

The structure of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). also contains other interesting chemical elements:

Arsenic	(As)	1 atom
Iron	(Fe)	1 atom

The binding sites of Calcium atom in the Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). (pdb code 1kzm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C)., PDB code: 1kzm:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:9.0 occ:1.00 O A:VAL46 2.3 11.6 1.0 OD1 A:ASP50 2.3 9.7 1.0 O A:ASP43 2.4 9.7 1.0 OD1 A:ASP43 2.4 11.1 1.0 OG A:SER52 2.4 11.3 1.0 O A:HOH1031 2.5 11.1 1.0 O A:GLY48 2.5 11.8 1.0 C A:ASP43 3.3 9.6 1.0 CG A:ASP50 3.4 11.8 1.0 C A:VAL46 3.4 11.7 1.0 CG A:ASP43 3.5 13.7 1.0 CB A:SER52 3.6 9.0 1.0 C A:GLY48 3.7 12.8 1.0 CA A:ASP43 3.7 11.5 1.0 N A:SER52 3.9 10.4 1.0 N A:ASP50 3.9 11.2 1.0 OD2 A:ASP50 3.9 8.8 1.0 CA A:VAL46 4.2 10.1 1.0 CB A:VAL46 4.2 11.6 1.0 CB A:ASP43 4.3 12.2 1.0 CA A:SER52 4.3 11.3 1.0 N A:GLY48 4.3 13.6 1.0 C A:ASN47 4.3 15.4 1.0 N A:VAL46 4.3 9.8 1.0 N A:CYS44 4.4 10.6 1.0 N A:ASN47 4.5 11.9 1.0 OD2 A:ASP43 4.5 11.6 1.0 N A:ALA51 4.5 9.4 1.0 N A:ILE53 4.5 12.1 0.6 N A:ILE53 4.5 12.0 0.4 CB A:ASN47 4.6 15.6 1.0 CA A:CYS49 4.6 12.4 1.0 CB A:ASP50 4.6 10.6 1.0 N A:CYS49 4.6 11.9 1.0 CA A:GLY48 4.6 12.6 1.0 CA A:ASP50 4.6 11.2 1.0 O A:ASN47 4.6 17.8 1.0 OE1 A:GLU64 4.7 13.3 1.0 CA A:ASN47 4.7 15.2 1.0 OE2 A:GLU64 4.7 13.5 1.0 C A:ASP50 4.7 11.1 1.0 C A:CYS49 4.8 11.9 1.0 O A:GLU42 4.8 11.4 1.0 CA A:CYS44 4.8 12.3 1.0 C A:SER52 4.9 11.4 1.0 CG1 A:VAL46 4.9 8.8 1.0 C A:ALA51 5.0 11.3 1.0

Calcium binding site 2 out of 2 in the Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C).


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (Hrp C). within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:10.5 occ:1.00 O A:THR171 2.3 10.4 1.0 OD2 A:ASP222 2.3 14.9 1.0 O A:ILE228 2.4 10.9 1.0 O A:THR225 2.4 12.4 1.0 OD1 A:ASP230 2.4 10.7 1.0 OG1 A:THR225 2.4 12.2 1.0 OG1 A:THR171 2.5 11.1 1.0 C A:THR171 3.3 10.2 1.0 CG A:ASP230 3.3 12.2 1.0 CG A:ASP222 3.4 14.6 1.0 C A:THR225 3.4 13.0 1.0 CB A:THR225 3.5 12.7 1.0 C A:ILE228 3.6 12.2 1.0 CB A:THR171 3.6 10.3 1.0 OD2 A:ASP230 3.6 10.5 1.0 CA A:THR171 3.8 10.0 1.0 CB A:ASP222 3.9 11.4 1.0 CA A:THR225 3.9 11.7 1.0 N A:ASP230 4.1 11.2 1.0 N A:THR225 4.3 11.8 1.0 N A:ILE228 4.3 11.8 1.0 CG2 A:THR171 4.3 9.6 1.0 CB A:LYS232 4.3 14.7 1.0 CA A:ILE228 4.4 12.8 1.0 OD1 A:ASP222 4.4 12.4 1.0 N A:PHE172 4.5 11.3 1.0 N A:PRO226 4.6 12.7 1.0 N A:PHE229 4.6 10.0 1.0 CB A:ILE228 4.6 13.9 1.0 O A:ASP230 4.6 11.5 1.0 CB A:ASP230 4.6 10.7 1.0 CG A:LYS232 4.6 17.9 1.0 CA A:PHE229 4.7 10.9 1.0 CA A:ASP230 4.8 11.0 1.0 CG2 A:THR225 4.8 11.7 1.0 C A:PHE229 4.8 11.9 1.0 CA A:PHE172 4.9 12.2 1.0 C A:ASP230 4.9 10.3 1.0

K.Meno, S.Jennings, A.T.Smith, A.Henriksen, M.Gajhede. Structural Analysis of the Two Horseradish Peroxidase Catalytic Residue Variants H42E and R38S/H42E: Implications For the Catalytic Cycle. Acta Crystallogr.,Sect.D V. 58 1803 2002.
ISSN: ISSN 0907-4449
PubMed: 12351824
DOI: 10.1107/S090744490201329X