Calcium in PDB 4fdq: The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase

All present enzymatic activity of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase:
1.11.1.16;

The structure of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase, PDB code: 4fdq was solved by M.J.Mate, A.Romero, F.J.Ruiz-Duenas, A.T.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.12 / 1.60
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	96.230, 96.230, 98.730, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 17.9

The structure of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase (pdb code 4fdq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase, PDB code: 4fdq:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:7.3 occ:1.00 O A:HOH509 2.4 7.1 1.0 OD1 A:ASP48 2.4 6.9 1.0 OG A:SER64 2.4 7.0 1.0 O A:GLY60 2.4 6.5 1.0 OD1 A:ASP62 2.4 6.4 1.0 O A:ASP48 2.5 6.7 1.0 O A:HOH534 2.5 8.7 1.0 CG A:ASP48 3.4 8.2 1.0 C A:ASP48 3.4 6.6 1.0 CG A:ASP62 3.5 6.5 1.0 CB A:SER64 3.5 6.7 1.0 C A:GLY60 3.6 5.5 1.0 CA A:ASP48 3.8 5.4 1.0 N A:SER64 4.0 6.8 1.0 OD2 A:ASP62 4.0 9.0 1.0 OD2 A:ASP48 4.2 7.9 1.0 O A:HOH513 4.2 7.5 1.0 N A:ASP62 4.2 7.0 1.0 CB A:ASP48 4.2 5.4 1.0 N A:GLY60 4.3 7.6 1.0 CA A:SER64 4.3 7.6 1.0 CA A:GLY60 4.3 7.5 1.0 N A:ILE65 4.4 6.8 1.0 O A:GLY51 4.5 7.7 1.0 N A:ALA49 4.5 5.5 1.0 OE2 A:GLU72 4.5 7.5 1.0 N A:GLY63 4.6 5.8 1.0 OE1 A:GLU72 4.7 9.0 1.0 N A:ALA61 4.7 6.2 1.0 CB A:ASP62 4.7 7.0 1.0 C A:SER64 4.8 7.6 1.0 CA A:GLY51 4.8 6.5 1.0 CA A:ASP62 4.9 7.4 1.0 CA A:ALA61 4.9 7.0 1.0 N A:GLY51 4.9 6.8 1.0 CA A:ALA49 4.9 6.0 1.0 C A:GLY59 4.9 7.1 1.0 O A:HIS47 4.9 7.5 1.0

Calcium binding site 2 out of 2 in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:7.0 occ:1.00 O A:SER170 2.4 5.9 1.0 O A:THR189 2.4 7.1 1.0 OD2 A:ASP187 2.4 6.2 1.0 OD1 A:ASP194 2.5 7.2 1.0 O A:VAL192 2.5 6.4 1.0 OG A:SER170 2.5 5.7 1.0 OG1 A:THR189 2.5 7.1 1.0 OD1 A:ASP187 2.7 7.6 1.0 CG A:ASP187 2.9 6.1 1.0 C A:THR189 3.3 6.8 1.0 C A:SER170 3.4 4.3 1.0 CG A:ASP194 3.4 9.0 1.0 CB A:THR189 3.5 7.2 1.0 CB A:SER170 3.6 6.1 1.0 CA A:SER170 3.7 5.2 1.0 C A:VAL192 3.7 6.6 1.0 OD2 A:ASP194 3.9 7.8 1.0 CA A:THR189 3.9 7.3 1.0 N A:ASP194 4.1 5.6 1.0 N A:THR189 4.2 6.0 1.0 N A:PRO190 4.3 5.5 1.0 N A:VAL192 4.4 5.6 1.0 CB A:VAL192 4.4 9.1 1.0 CA A:PRO190 4.5 6.4 1.0 CB A:ASP187 4.5 7.5 1.0 CA A:VAL192 4.5 6.8 1.0 O A:ASP194 4.5 7.5 1.0 O A:HOH512 4.6 8.7 1.0 CB A:GLN196 4.6 6.3 1.0 N A:ILE171 4.6 5.5 1.0 CB A:ASP194 4.6 6.9 1.0 N A:PHE193 4.7 6.0 1.0 CA A:PHE193 4.7 7.1 1.0 CA A:ASP194 4.8 7.2 1.0 CG2 A:ILE171 4.8 5.9 1.0 C A:ASP194 4.8 7.3 1.0 CG2 A:THR189 4.9 8.3 1.0 C A:PHE193 4.9 7.0 1.0 C A:PRO190 5.0 6.3 1.0

M.Morales, M.J.Mate, A.Romero, M.J.Martinez, A.T.Martinez, F.J.Ruiz-Duenas. Two Oxidation Sites For Low Redox Potential Substrates: A Directed Mutagenesis, Kinetic, and Crystallographic Study on Pleurotus Eryngii Versatile Peroxidase. J.Biol.Chem. V. 287 41053 2012.
ISSN: ISSN 0021-9258
PubMed: 23071108
DOI: 10.1074/JBC.M112.405548