Calcium in PDB 8qwt: Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion

All present enzymatic activity of Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion:
1.11.1.13;

The structure of Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion, PDB code: 8qwt was solved by E.Santillana, A.Romero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.76 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.79, 56.64, 109.51, 90, 90, 90
R / Rfree (%)	16.3 / 18.9

The structure of Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Magnesium	(Mg)	3 atoms
Manganese	(Mn)	1 atom

The binding sites of Calcium atom in the Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion (pdb code 8qwt). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion, PDB code: 8qwt:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca403 b:10.8 occ:1.00 O A:THR171 2.4 11.2 1.0 O A:THR190 2.4 12.2 1.0 OD1 A:ASP195 2.4 10.6 1.0 OG1 A:THR171 2.5 9.6 1.0 OG1 A:THR190 2.5 12.5 1.0 OD2 A:ASP188 2.5 12.1 1.0 O A:THR193 2.5 10.7 1.0 OD1 A:ASP188 2.8 11.9 1.0 CG A:ASP188 3.0 12.1 1.0 C A:THR190 3.2 11.8 1.0 C A:THR171 3.3 9.3 1.0 CG A:ASP195 3.5 12.3 1.0 CB A:THR190 3.5 12.8 1.0 CB A:THR171 3.6 10.1 1.0 CA A:THR171 3.7 9.7 1.0 C A:THR193 3.7 11.1 1.0 CA A:THR190 3.9 11.7 1.0 OD2 A:ASP195 3.9 13.0 1.0 N A:ASP195 4.2 10.8 1.0 N A:VAL191 4.2 12.2 1.0 N A:THR190 4.3 10.9 1.0 CG2 A:THR171 4.4 8.9 1.0 CB A:GLN197 4.4 12.1 1.0 N A:THR193 4.4 13.3 1.0 CA A:THR193 4.5 12.6 1.0 CB A:ASP188 4.5 11.1 1.0 O A:ASP195 4.5 11.7 1.0 CA A:VAL191 4.5 13.1 1.0 CB A:THR193 4.5 13.4 1.0 N A:ILE172 4.5 10.4 1.0 O A:HOH629 4.6 16.8 1.0 CB A:ASP195 4.7 11.6 1.0 N A:PHE194 4.7 10.5 1.0 CA A:ASP195 4.8 10.5 1.0 CG2 A:THR190 4.8 14.2 1.0 C A:ASP195 4.8 11.5 1.0 CA A:PHE194 4.9 10.5 1.0 CG2 A:ILE172 4.9 13.0 1.0 C A:VAL191 4.9 12.9 1.0

Calcium binding site 2 out of 2 in the Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ligninolytic Manganese Peroxidase Cst-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca404 b:12.7 occ:1.00 OD1 A:ASP48 2.3 12.1 1.0 O A:HOH552 2.3 14.7 1.0 OG A:SER65 2.4 13.1 1.0 OD1 A:ASP63 2.4 12.9 1.0 O A:HOH579 2.5 13.1 1.0 O A:ASP48 2.5 11.3 1.0 O A:GLY61 2.5 13.9 1.0 CG A:ASP48 3.3 12.7 1.0 C A:ASP48 3.4 11.9 1.0 CG A:ASP63 3.5 14.4 1.0 CB A:SER65 3.6 14.4 1.0 C A:GLY61 3.7 14.0 1.0 CA A:ASP48 3.8 11.3 1.0 N A:SER65 3.9 13.1 1.0 OD2 A:ASP48 4.0 14.9 1.0 OD2 A:ASP63 4.1 16.5 1.0 CB A:ASP48 4.1 12.1 1.0 O A:HOH555 4.2 14.8 1.0 N A:ASP63 4.2 13.8 1.0 CA A:SER65 4.2 13.8 1.0 N A:GLY61 4.4 14.3 1.0 N A:ILE66 4.4 13.7 1.0 CA A:GLY61 4.5 13.9 1.0 N A:GLY64 4.5 12.5 1.0 O A:GLY51 4.5 16.0 1.0 N A:ALA49 4.5 11.8 1.0 OE2 A:GLU73 4.6 15.9 1.0 CB A:ASP63 4.7 14.3 1.0 N A:ALA62 4.7 12.9 1.0 C A:SER65 4.8 15.3 1.0 CA A:ASP63 4.8 14.1 1.0 CA A:GLY51 4.8 13.7 1.0 OE1 A:GLU73 4.9 16.5 1.0 CA A:ALA49 4.9 11.5 1.0 C A:GLY64 4.9 13.7 1.0 CA A:ALA62 4.9 12.8 1.0 O A:HOH541 5.0 13.9 1.0 C A:ASP63 5.0 13.4 1.0

M.I.Sanchez-Ruiz, E.Santillana, D.Linde, A.Romero, A.T.Martinez, F.J.Ruiz-Duenas. Structure-Function Characterization of Two Enzymes From Novel Subfamilies of Manganese Peroxidases Secreted By the Lignocellulose-Degrading Agaricales Fungi Agrocybe Pediades and Cyathus Striatus. Biotechnol Biofuels Bioprod V. 17 74 2024.
ISSN: ISSN 2731-3654
PubMed: 38824538
DOI: 10.1186/S13068-024-02517-1