Calcium in PDB 4bm3: Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III

All present enzymatic activity of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III:
1.11.1.13;

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III, PDB code: 4bm3 was solved by F.J.Medrano, A.Romero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.366 / 1.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	124.250, 86.530, 40.300, 90.00, 107.82, 90.00
R / Rfree (%)	21.04 / 24.22

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III (pdb code 4bm3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III, PDB code: 4bm3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:14.0 occ:1.00 OD1 A:ASP49 2.5 19.1 1.0 O A:ASP49 2.5 13.2 1.0 O A:HOH2077 2.5 13.0 1.0 OG A:SER71 2.5 14.1 1.0 OD1 A:ASP69 2.6 18.4 1.0 O A:GLY67 2.6 18.5 1.0 O A:HOH2083 2.6 17.6 1.0 C A:ASP49 3.4 13.3 1.0 CG A:ASP49 3.5 15.5 1.0 CG A:ASP69 3.5 19.0 1.0 CB A:SER71 3.6 12.8 1.0 C A:GLY67 3.7 16.1 1.0 CA A:ASP49 3.8 11.2 1.0 OD2 A:ASP69 3.9 15.0 1.0 N A:SER71 4.0 16.8 1.0 O A:HOH2103 4.1 16.4 1.0 N A:ASP69 4.2 13.6 1.0 OD2 A:ASP49 4.2 17.1 1.0 CB A:ASP49 4.3 13.8 1.0 CA A:SER71 4.3 21.2 1.0 N A:GLY67 4.3 15.5 1.0 CA A:GLY67 4.4 14.1 1.0 N A:ILE72 4.4 18.1 1.0 O A:GLY52 4.5 14.7 1.0 N A:ALA50 4.5 12.2 1.0 N A:ALA68 4.7 14.5 1.0 OE2 A:GLU79 4.7 17.3 1.0 CB A:ASP69 4.7 18.8 1.0 N A:GLY70 4.7 15.8 1.0 OE1 A:GLU79 4.8 16.0 1.0 C A:SER71 4.8 19.0 1.0 CA A:ASP69 4.8 18.9 1.0 CA A:ALA68 4.8 12.9 1.0 O A:HIS48 4.9 14.4 1.0 CA A:ALA50 5.0 13.0 1.0 C A:GLY66 5.0 15.8 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form III within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:13.7 occ:1.00 OG A:SER177 2.5 10.6 1.0 O A:THR196 2.5 14.0 1.0 O A:SER177 2.5 13.8 1.0 O A:ASP199 2.5 14.2 1.0 OD2 A:ASP194 2.5 13.0 1.0 OD1 A:ASP201 2.6 14.4 1.0 OG1 A:THR196 2.7 17.4 1.0 OD1 A:ASP194 2.7 14.4 1.0 CG A:ASP194 3.0 17.5 1.0 C A:THR196 3.3 16.1 1.0 CG A:ASP201 3.4 14.1 1.0 C A:SER177 3.4 14.1 1.0 CB A:SER177 3.6 16.6 1.0 CB A:THR196 3.7 15.9 1.0 C A:ASP199 3.7 11.9 1.0 CA A:SER177 3.7 15.7 1.0 OD2 A:ASP201 3.8 14.6 1.0 CA A:THR196 3.9 14.0 1.0 N A:ASP201 4.1 14.0 1.0 N A:THR196 4.2 12.4 1.0 N A:PRO197 4.2 14.4 1.0 CA A:ASP199 4.4 12.8 1.0 CB A:ASP199 4.4 11.6 1.0 O A:ASP201 4.4 14.2 1.0 N A:ASP199 4.4 12.9 1.0 CA A:PRO197 4.5 14.3 1.0 CB A:ASP194 4.5 16.7 1.0 CB A:ASP201 4.6 10.1 1.0 N A:VAL178 4.6 15.7 1.0 N A:PHE200 4.7 11.5 1.0 O A:HOH2239 4.7 14.7 1.0 CA A:ASP201 4.7 12.4 1.0 C A:ASP201 4.8 12.6 1.0 CB A:GLN203 4.8 11.7 1.0 CG1 A:VAL178 4.8 12.9 1.0 CA A:PHE200 4.8 9.6 1.0 CG2 A:THR196 5.0 11.9 1.0 C A:PHE200 5.0 15.2 1.0

E.Fernandez-Fueyo, F.J.Ruiz-Duenas, M.J.Martinez, A.Romero, K.E.Hammel, F.J.Medrano, A.T.Martinez. Ligninolytic Peroxidase Genes in the Oyster Mushroom Genome: Heterologous Expression, Molecular Structure, Catalytic and Stability Properties, and Lignin-Degrading Ability. Biotechnol.Biofuels V. 7 2 2014.
ISSN: ISSN 1754-6834
PubMed: 24387130
DOI: 10.1186/1754-6834-7-2