Calcium in PDB 4bm0: Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII

All present enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII:
1.11.1.16;

The structure of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII, PDB code: 4bm0 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)	48.350 / 2.20
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	96.700, 96.700, 38.400, 90.00, 90.00, 90.00
R / Rfree (%)	22.79 / 27.12

The structure of Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII (pdb code 4bm0). 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 Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII, PDB code: 4bm0:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII


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 Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:50.0 occ:1.00 O A:GLY61 3.0 44.8 1.0 OG A:SER65 3.0 37.4 1.0 O A:ASP49 3.0 47.3 1.0 OD1 A:ASP63 3.1 38.2 1.0 OD1 A:ASP49 3.3 35.9 1.0 O A:GLY52 3.5 40.4 1.0 CB A:SER134 3.6 35.2 1.0 N A:GLY61 3.7 42.4 1.0 CG A:ASP63 3.8 39.6 1.0 CB A:SER65 3.8 37.2 1.0 C A:GLY61 3.9 39.4 1.0 OD2 A:ASP63 3.9 39.4 1.0 CA A:GLY52 4.0 36.2 1.0 C A:ASP49 4.1 41.1 1.0 OG A:SER134 4.1 38.8 1.0 CA A:GLY61 4.1 42.3 1.0 C A:GLY52 4.1 37.0 1.0 N A:GLY60 4.2 42.2 1.0 C A:GLY60 4.3 42.6 1.0 CA A:SER134 4.4 33.8 1.0 N A:GLY52 4.4 36.2 1.0 CG A:ASP49 4.4 32.8 1.0 OE1 A:GLU73 4.5 48.9 1.0 CA A:ASP49 4.6 30.2 1.0 CA A:GLY60 4.6 40.8 1.0 N A:SER134 4.7 32.7 1.0 N A:SER65 4.8 41.7 1.0 OE2 A:GLU73 4.9 54.1 1.0 CA A:SER65 4.9 41.4 1.0 N A:ASP63 5.0 35.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII


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 Fungal Versatile Peroxidase I From Pleurotus Ostreatus - Crystal Form VII within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:39.4 occ:1.00 O A:SER171 2.8 28.7 1.0 OD1 A:ASP195 2.9 38.4 1.0 OG1 A:THR190 2.9 35.8 1.0 OD2 A:ASP188 2.9 55.5 1.0 O A:THR190 2.9 39.9 1.0 O A:VAL193 3.0 34.8 1.0 OD1 A:ASP188 3.0 58.1 1.0 OG A:SER171 3.1 35.4 1.0 CG A:ASP188 3.2 53.8 1.0 C A:THR190 3.3 38.9 1.0 CB A:THR190 3.5 39.4 1.0 CG A:ASP195 3.6 36.9 1.0 C A:SER171 3.7 29.9 1.0 CA A:THR190 3.7 40.5 1.0 CB A:SER171 3.8 30.6 1.0 OD2 A:ASP195 3.8 34.4 1.0 CA A:SER171 3.9 32.0 1.0 N A:THR190 3.9 38.2 1.0 N A:PRO191 4.1 36.1 1.0 C A:VAL193 4.2 39.7 1.0 CB A:GLN197 4.2 27.2 1.0 N A:ASP195 4.2 34.2 1.0 O A:ASP195 4.5 33.4 1.0 CA A:PRO191 4.6 34.8 1.0 CB A:ASP188 4.6 46.7 1.0 O A:HOH2061 4.7 33.2 1.0 N A:PHE198 4.8 31.6 1.0 C A:ASP195 4.8 30.8 1.0 CB A:ASP195 4.8 33.0 1.0 N A:GLN197 4.8 32.7 1.0 CA A:ASP195 4.8 31.6 1.0 N A:ILE172 4.9 31.4 1.0 CA A:GLN197 4.9 30.6 1.0 CG2 A:THR190 5.0 42.1 1.0 CG A:GLN197 5.0 28.3 1.0 N A:VAL193 5.0 40.0 1.0 CA A:VAL193 5.0 38.9 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