Calcium in PDB 4bm2: Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form II

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

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form II, PDB code: 4bm2 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)	43.280 / 1.39
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	123.670, 86.560, 40.030, 90.00, 107.64, 90.00
R / Rfree (%)	22.1 / 24.45

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form II 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 II (pdb code 4bm2). 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 II, PDB code: 4bm2:
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 II


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 II within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:8.2 occ:1.00 OD1 A:ASP49 2.3 9.5 1.0 O A:HOH2099 2.4 10.0 1.0 O A:GLY67 2.4 8.3 1.0 OD1 A:ASP69 2.4 11.4 1.0 O A:HOH2093 2.4 11.6 1.0 O A:ASP49 2.5 8.4 1.0 OG A:SER71 2.5 10.5 1.0 C A:ASP49 3.4 7.1 1.0 CG A:ASP49 3.4 10.0 1.0 CG A:ASP69 3.5 10.7 1.0 CB A:SER71 3.6 8.1 1.0 C A:GLY67 3.6 8.1 1.0 CA A:ASP49 3.8 8.8 1.0 OD2 A:ASP69 4.0 10.2 1.0 N A:SER71 4.0 7.8 1.0 O A:HOH2120 4.1 9.6 1.0 N A:ASP69 4.1 10.8 1.0 OD2 A:ASP49 4.2 10.3 1.0 CB A:ASP49 4.2 9.2 1.0 CA A:SER71 4.3 8.1 1.0 N A:GLY67 4.3 8.4 1.0 CA A:GLY67 4.4 8.0 1.0 N A:ILE72 4.4 8.9 1.0 N A:ALA50 4.5 6.9 1.0 O A:GLY52 4.6 10.4 1.0 OE2 A:GLU79 4.6 10.3 1.0 N A:GLY70 4.7 8.3 1.0 N A:ALA68 4.7 7.7 1.0 CB A:ASP69 4.7 9.7 1.0 OE1 A:GLU79 4.7 9.5 1.0 CA A:ASP69 4.8 10.0 1.0 CA A:ALA68 4.8 9.8 1.0 C A:SER71 4.9 8.4 1.0 CA A:ALA50 4.9 11.0 1.0 CA A:GLY52 4.9 15.7 1.0 C A:GLY66 4.9 8.8 1.0 O A:HIS48 5.0 9.9 1.0 N A:GLY52 5.0 7.9 1.0 CB A:SER140 5.0 7.8 1.0 C A:ASP69 5.0 8.5 1.0

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


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 II within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:7.4 occ:1.00 O A:SER177 2.3 6.2 1.0 O A:THR196 2.4 9.4 1.0 OD2 A:ASP194 2.4 8.8 1.0 O A:ASP199 2.4 7.6 1.0 OG A:SER177 2.5 6.0 1.0 OD1 A:ASP201 2.5 8.2 1.0 OG1 A:THR196 2.6 9.8 1.0 OD1 A:ASP194 2.8 7.5 1.0 CG A:ASP194 3.0 5.3 1.0 C A:THR196 3.2 8.8 1.0 C A:SER177 3.3 5.9 1.0 CG A:ASP201 3.4 8.8 1.0 CB A:THR196 3.6 7.6 1.0 CB A:SER177 3.6 6.4 1.0 C A:ASP199 3.6 8.3 1.0 CA A:SER177 3.7 8.4 1.0 CA A:THR196 3.8 6.5 1.0 OD2 A:ASP201 3.8 7.1 1.0 N A:ASP201 4.1 6.7 1.0 N A:THR196 4.2 6.4 1.0 N A:PRO197 4.2 7.3 1.0 CB A:ASP199 4.3 8.3 1.0 CA A:ASP199 4.4 9.6 1.0 N A:ASP199 4.4 9.8 1.0 CA A:PRO197 4.5 7.3 1.0 CB A:ASP194 4.5 7.6 1.0 N A:VAL178 4.5 7.5 1.0 O A:HOH2285 4.5 9.2 1.0 O A:ASP201 4.5 6.9 1.0 CB A:ASP201 4.6 9.0 1.0 N A:PHE200 4.7 7.6 1.0 CA A:ASP201 4.7 7.5 1.0 C A:ASP201 4.8 5.7 1.0 CG1 A:VAL178 4.8 8.1 1.0 CB A:GLN203 4.9 11.3 1.0 CA A:PHE200 4.9 6.1 1.0 CG2 A:THR196 4.9 6.6 1.0 C A:PRO197 5.0 8.3 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