Calcium in PDB 4czn: Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora

All present enzymatic activity of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora:
1.11.1.13;

The structure of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora, PDB code: 4czn 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)	42.626 / 1.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.560, 108.560, 68.850, 90.00, 90.00, 90.00
R / Rfree (%)	13.44 / 15.11

The structure of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Sodium	(Na)	1 atom

The binding sites of Calcium atom in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora (pdb code 4czn). 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 the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora, PDB code: 4czn:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora


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 the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1369 b:6.8 occ:1.00 O A:THR174 2.4 7.4 1.0 O A:THR193 2.4 7.1 1.0 OD2 A:ASP191 2.4 7.3 1.0 OG1 A:THR174 2.5 7.1 1.0 OD1 A:ASP198 2.5 7.3 1.0 OG1 A:THR193 2.5 7.9 1.0 O A:THR196 2.5 7.3 1.0 OD1 A:ASP191 2.7 7.3 1.0 CG A:ASP191 2.9 7.0 1.0 C A:THR193 3.2 7.4 1.0 C A:THR174 3.3 6.7 1.0 H A:ASP198 3.4 8.6 1.0 HA A:THR174 3.4 7.6 1.0 CG A:ASP198 3.4 7.2 1.0 CB A:THR193 3.5 7.8 1.0 CB A:THR174 3.6 6.6 1.0 CA A:THR174 3.7 6.3 1.0 HB A:THR193 3.7 9.4 1.0 HB2 A:GLN200 3.7 9.5 1.0 HB A:THR196 3.7 10.0 1.0 H A:THR193 3.7 9.1 1.0 H A:THR196 3.7 9.3 1.0 C A:THR196 3.7 6.4 1.0 OD2 A:ASP198 3.8 7.7 1.0 CA A:THR193 3.9 7.1 1.0 HA A:PRO194 3.9 9.3 1.0 HG21 A:THR174 4.1 8.4 1.0 N A:ASP198 4.2 7.1 1.0 N A:THR193 4.2 7.6 1.0 N A:PRO194 4.2 7.9 1.0 HB A:THR174 4.3 7.9 1.0 HG21 A:ILE175 4.4 9.5 1.0 CG2 A:THR174 4.4 7.0 1.0 HA A:PHE197 4.4 9.0 1.0 CB A:ASP191 4.4 8.0 1.0 N A:THR196 4.4 7.7 1.0 H A:GLN200 4.5 8.7 1.0 H A:ILE201 4.5 8.6 1.0 CA A:THR196 4.5 7.8 1.0 CA A:PRO194 4.5 7.7 1.0 CB A:THR196 4.5 8.3 1.0 O A:ASP198 4.5 7.6 1.0 N A:ILE175 4.5 6.6 1.0 O A:HOH2351 4.6 11.0 1.0 HA A:ILE175 4.6 7.6 1.0 CB A:GLN200 4.6 7.9 1.0 CB A:ASP198 4.7 7.5 1.0 HG22 A:THR174 4.7 8.4 1.0 HB2 A:ASP191 4.7 9.6 1.0 HB3 A:ASP191 4.8 9.6 1.0 HA A:THR193 4.8 8.5 1.0 N A:PHE197 4.8 7.0 1.0 HG23 A:ILE175 4.8 9.5 1.0 CA A:ASP198 4.8 7.5 1.0 C A:ASP198 4.8 7.1 1.0 CG2 A:THR193 4.9 8.3 1.0 HG2 A:GLN200 4.9 9.5 1.0 HB A:ILE201 4.9 9.8 1.0 CA A:PHE197 4.9 7.5 1.0 HG3 A:GLN200 5.0 9.5 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora


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 the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1370 b:8.9 occ:1.00 OD1 A:ASP47 2.3 9.7 1.0 O A:HOH2122 2.3 9.7 1.0 OD1 A:ASP64 2.4 9.8 1.0 O A:HOH2114 2.4 9.4 1.0 O A:ASP47 2.4 9.4 1.0 O A:GLY62 2.4 9.4 1.0 OG A:SER66 2.5 10.0 1.0 HA A:ASP47 3.2 10.5 1.0 H A:SER66 3.2 12.1 1.0 H A:ASP64 3.3 11.0 1.0 C A:ASP47 3.3 8.1 1.0 CG A:ASP47 3.4 8.8 1.0 CG A:ASP64 3.5 9.9 1.0 HB1 A:ALA50 3.6 11.5 1.0 HB3 A:SER66 3.6 12.4 1.0 CB A:SER66 3.6 10.3 1.0 C A:GLY62 3.6 9.2 1.0 CA A:ASP47 3.7 8.7 1.0 OD2 A:ASP64 4.0 10.3 1.0 N A:SER66 4.0 10.1 1.0 H A:MET67 4.1 12.9 1.0 N A:ASP64 4.1 9.2 1.0 CB A:ASP47 4.2 8.8 1.0 H A:GLY62 4.2 12.1 1.0 O A:HOH2154 4.2 10.7 1.0 OD2 A:ASP47 4.3 9.8 1.0 HA A:ALA63 4.3 10.3 1.0 HG2 A:MET67 4.3 12.8 1.0 H A:GLY65 4.3 12.6 1.0 HB2 A:SER66 4.3 12.4 1.0 HA2 A:GLY62 4.3 11.4 1.0 N A:GLY62 4.3 10.1 1.0 CA A:GLY62 4.3 9.5 1.0 CA A:SER66 4.4 10.3 1.0 OE1 A:GLU74 4.5 11.9 1.0 HA A:ALA48 4.5 10.4 1.0 N A:ALA48 4.5 8.4 1.0 CB A:ALA50 4.5 9.6 1.0 O A:ALA50 4.6 9.8 1.0 OE2 A:GLU74 4.6 10.8 1.0 H A:ALA50 4.6 10.7 1.0 N A:GLY65 4.6 10.5 1.0 N A:ALA63 4.6 9.3 1.0 CB A:ASP64 4.7 10.5 1.0 HB3 A:ALA136 4.7 13.6 1.0 N A:MET67 4.7 10.8 1.0 HB3 A:ASP47 4.8 10.6 1.0 O A:HIS46 4.8 9.6 1.0 H A:GLY61 4.8 12.7 1.0 CA A:ASP64 4.8 10.1 1.0 HB2 A:ASP47 4.8 10.6 1.0 CA A:ALA63 4.8 8.6 1.0 HB2 A:ALA50 4.9 11.5 1.0 HB3 A:ALA50 4.9 11.5 1.0 C A:ASP64 4.9 10.6 1.0 HB3 A:ASP64 5.0 12.6 1.0 CA A:ALA48 5.0 8.7 1.0 C A:GLY61 5.0 9.7 1.0 CD A:GLU74 5.0 10.9 1.0

E.Fernandez-Fueyo, S.Acebes, F.J.Ruiz-Duenas, M.J.Martinez, A.Romero, F.J.Medrano, V.Guallar, A.T.Martinez. Structural Implications of the C-Terminal Tail in the Catalytic and Stability Properties of Manganese Peroxidases From Ligninolytic Fungi Acta Crystallogr.,Sect.D V. 70 3253 2014.
ISSN: ISSN 0907-4449
PubMed: 25478843
DOI: 10.1107/S1399004714022755