Calcium in PDB 4bm4: Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV

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

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV, PDB code: 4bm4 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)	43.250 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	123.870, 86.500, 41.400, 90.00, 108.05, 90.00
R / Rfree (%)	22.49 / 29.71

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV 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 IV (pdb code 4bm4). 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 IV, PDB code: 4bm4:
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 IV


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 IV within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:26.4 occ:1.00 O A:ASP49 2.7 14.4 1.0 OG A:SER71 2.8 14.2 1.0 O A:HOH2024 2.8 20.3 1.0 OD1 A:ASP69 2.9 31.5 1.0 O A:HOH2029 2.9 18.6 1.0 OD1 A:ASP49 2.9 40.4 1.0 O A:GLY67 3.0 43.3 1.0 CG A:ASP49 3.6 41.0 1.0 C A:ASP49 3.6 43.2 1.0 CA A:ASP49 3.8 34.0 1.0 CB A:SER71 3.9 38.2 1.0 N A:SER71 3.9 41.8 1.0 CG A:ASP69 3.9 32.7 1.0 OE2 A:GLU79 3.9 37.1 1.0 C A:GLY67 3.9 36.4 1.0 O A:HOH2036 4.1 18.9 1.0 OD2 A:ASP49 4.2 38.9 1.0 N A:ILE72 4.3 13.0 1.0 CB A:ASP49 4.3 36.9 1.0 N A:ASP69 4.4 33.8 1.0 CA A:SER71 4.4 40.5 1.0 OD2 A:ASP69 4.4 31.2 1.0 CA A:GLY67 4.6 28.8 1.0 N A:GLY70 4.6 36.5 1.0 N A:GLY67 4.6 32.8 1.0 CB A:SER140 4.6 28.2 1.0 O A:GLY52 4.8 33.7 1.0 C A:SER71 4.8 28.9 1.0 N A:ALA50 4.8 37.4 1.0 CA A:GLY52 4.8 31.2 1.0 CD A:GLU79 4.8 29.7 1.0 O A:HIS48 4.8 29.4 1.0 OE1 A:GLU79 4.9 22.8 1.0 N A:ALA68 4.9 30.1 1.0 C A:GLY70 4.9 41.4 1.0 N A:GLY52 5.0 36.1 1.0

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


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 IV within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:19.4 occ:1.00 O A:SER177 2.7 14.6 1.0 OD1 A:ASP201 2.7 13.8 1.0 O A:THR196 2.8 29.6 1.0 OG A:SER177 2.8 19.8 1.0 O A:ASP199 2.8 37.7 1.0 OG1 A:THR196 2.8 39.1 1.0 OD2 A:ASP194 2.9 33.9 1.0 OD1 A:ASP194 3.0 18.9 1.0 CB A:SER177 3.3 33.3 1.0 C A:SER177 3.4 19.8 1.0 CG A:ASP194 3.4 34.9 1.0 C A:THR196 3.5 25.0 1.0 CA A:SER177 3.5 25.9 1.0 CG A:ASP201 3.5 36.7 1.0 C A:ASP199 3.7 38.4 1.0 N A:ASP201 3.8 46.7 1.0 CB A:THR196 3.9 23.6 1.0 OD2 A:ASP201 4.0 40.3 1.0 O A:ASP201 4.1 18.7 1.0 CA A:THR196 4.1 23.1 1.0 N A:PRO197 4.3 15.8 1.0 CB A:ASP199 4.3 26.6 1.0 N A:THR196 4.4 37.4 1.0 CA A:ASP199 4.5 34.5 1.0 CA A:PRO197 4.5 26.7 1.0 CA A:ASP201 4.5 46.9 1.0 N A:ASP199 4.6 33.3 1.0 N A:VAL178 4.6 24.5 1.0 CB A:ASP201 4.6 45.6 1.0 C A:ASP201 4.6 38.3 1.0 N A:PHE200 4.6 32.6 1.0 CA A:PHE200 4.6 30.2 1.0 C A:PHE200 4.7 36.3 1.0 CB A:GLN203 4.8 34.1 1.0 O A:HOH2108 4.9 19.8 1.0 CB A:ASP194 4.9 33.5 1.0 N A:SER177 4.9 33.2 1.0 N A:SER198 4.9 47.6 1.0 C A:PRO197 5.0 34.9 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