Calcium in PDB 6iss: Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239

All present enzymatic activity of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239:
1.11.1.14;

The structure of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239, PDB code: 6iss was solved by H.Seo, H.Son, K.-J.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.49 / 1.53
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	72.959, 93.740, 227.371, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.6

The structure of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239 also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Calcium atom in the Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239 (pdb code 6iss). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239, PDB code: 6iss:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:12.1 occ:1.00 OD1 A:ASP48 2.3 11.3 1.0 O A:HOH623 2.3 13.9 1.0 O A:GLY66 2.3 11.8 1.0 OD1 A:ASP68 2.4 12.3 1.0 OG A:SER70 2.4 12.5 1.0 O A:ASP48 2.5 12.3 1.0 O A:HOH567 2.5 13.6 1.0 C A:ASP48 3.4 11.5 1.0 CG A:ASP48 3.4 13.0 1.0 CG A:ASP68 3.5 14.9 1.0 CB A:SER70 3.5 14.1 1.0 C A:GLY66 3.6 11.6 1.0 CA A:ASP48 3.8 11.6 1.0 N A:SER70 3.9 13.5 1.0 OD2 A:ASP68 3.9 14.5 1.0 N A:ASP68 4.0 12.0 1.0 CB A:ASP48 4.2 11.6 1.0 O A:HOH553 4.2 14.6 1.0 CA A:SER70 4.3 13.8 1.0 OD2 A:ASP48 4.3 12.4 1.0 CA A:GLY66 4.3 13.1 1.0 N A:GLY66 4.3 13.8 1.0 N A:ILE71 4.4 14.0 1.0 CB A:ALA51 4.5 15.1 1.0 O A:ALA51 4.5 14.3 1.0 N A:GLY69 4.5 11.6 1.0 N A:CYS49 4.5 11.5 1.0 N A:CYS67 4.6 13.0 1.0 OE2 A:GLU78 4.6 14.8 1.0 CB A:ASP68 4.7 13.0 1.0 OE1 A:GLU78 4.8 14.1 1.0 CA A:ASP68 4.8 13.2 1.0 CA A:CYS67 4.8 12.3 1.0 C A:SER70 4.8 13.9 1.0 O A:HIS47 4.9 12.2 1.0 C A:GLY65 4.9 14.5 1.0 C A:CYS67 4.9 12.7 1.0 C A:ASP68 4.9 11.3 1.0 C A:GLY69 4.9 11.5 1.0

Calcium binding site 2 out of 4 in the Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca403 b:8.3 occ:1.00 O A:THR196 2.4 9.8 1.0 O A:ILE199 2.4 9.4 1.0 O A:SER177 2.4 8.1 1.0 OD1 A:ASP201 2.4 9.3 1.0 OG A:SER177 2.5 8.2 1.0 OG1 A:THR196 2.5 9.7 1.0 OD2 A:ASP194 2.5 8.4 1.0 OD1 A:ASP194 2.7 9.1 1.0 CG A:ASP194 3.0 8.8 1.0 C A:THR196 3.2 9.0 1.0 CG A:ASP201 3.3 10.2 1.0 C A:SER177 3.4 8.9 1.0 CB A:THR196 3.6 9.3 1.0 CB A:SER177 3.6 8.4 1.0 C A:ILE199 3.6 9.0 1.0 CA A:SER177 3.7 8.4 1.0 OD2 A:ASP201 3.7 11.0 1.0 CA A:THR196 3.9 9.0 1.0 N A:ASP201 4.1 9.6 1.0 N A:PRO197 4.2 9.1 1.0 N A:THR196 4.3 9.5 1.0 CA A:ILE199 4.4 9.9 1.0 N A:ILE199 4.4 9.8 1.0 CA A:PRO197 4.5 9.0 1.0 CB A:ASP194 4.5 9.3 1.0 CB A:ILE199 4.5 11.0 1.0 CB A:ASP201 4.6 9.9 1.0 O A:ASP201 4.6 9.9 1.0 N A:VAL178 4.6 9.1 1.0 O A:HOH694 4.6 9.7 1.0 CB A:GLN203 4.6 9.7 1.0 N A:PHE200 4.6 8.9 1.0 CA A:ASP201 4.7 9.6 1.0 CA A:PHE200 4.8 8.9 1.0 C A:ASP201 4.8 9.7 1.0 CG1 A:VAL178 4.8 9.6 1.0 CG2 A:THR196 4.9 9.6 1.0 C A:PHE200 4.9 9.3 1.0 C A:PRO197 5.0 8.2 1.0

Calcium binding site 3 out of 4 in the Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239 within 5.0Å range: probe atom residue distance (Å) B Occ G:Ca402 b:15.4 occ:1.00 OD1 G:ASP48 2.2 16.3 1.0 O G:HOH625 2.3 17.6 1.0 OG G:SER70 2.4 16.0 1.0 OD1 G:ASP68 2.4 18.5 1.0 O G:GLY66 2.4 15.6 1.0 O G:ASP48 2.4 15.1 1.0 O G:HOH579 2.5 16.2 1.0 CG G:ASP48 3.4 15.6 1.0 C G:ASP48 3.4 13.8 1.0 CG G:ASP68 3.4 18.0 1.0 CB G:SER70 3.5 17.6 1.0 C G:GLY66 3.6 15.5 1.0 CA G:ASP48 3.8 13.3 1.0 OD2 G:ASP68 3.9 17.0 1.0 N G:SER70 3.9 17.1 1.0 N G:ASP68 4.1 16.9 1.0 CB G:ASP48 4.2 13.9 1.0 CA G:SER70 4.2 16.9 1.0 OD2 G:ASP48 4.2 14.9 1.0 O G:HOH553 4.3 17.7 1.0 N G:GLY66 4.3 18.5 1.0 CA G:GLY66 4.4 16.6 1.0 O G:ALA51 4.4 18.2 1.0 N G:ILE71 4.5 16.1 1.0 CB G:ALA51 4.5 15.3 1.0 N G:CYS49 4.6 13.0 1.0 OE2 G:GLU78 4.6 19.1 1.0 CB G:ASP68 4.6 17.8 1.0 N G:CYS67 4.7 14.5 1.0 N G:GLY69 4.7 16.8 1.0 OE1 G:GLU78 4.7 18.6 1.0 C G:SER70 4.8 17.2 1.0 CA G:ASP68 4.8 16.7 1.0 CA G:CYS67 4.8 15.0 1.0 O G:HIS47 4.9 14.0 1.0 C G:GLY65 4.9 18.1 1.0 C G:ASP68 5.0 19.1 1.0 C G:GLY69 5.0 14.8 1.0

Calcium binding site 4 out of 4 in the Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Lignin Peroxidase H8 Triple Mutant S49C/A67C/H239 within 5.0Å range: probe atom residue distance (Å) B Occ G:Ca403 b:8.1 occ:1.00 O G:SER177 2.4 7.3 1.0 O G:THR196 2.4 7.8 1.0 OD2 G:ASP194 2.4 7.6 1.0 O G:ILE199 2.4 8.7 1.0 OD1 G:ASP201 2.5 8.0 1.0 OG G:SER177 2.5 7.2 1.0 OG1 G:THR196 2.5 8.7 1.0 OD1 G:ASP194 2.7 7.6 1.0 CG G:ASP194 2.9 7.8 1.0 C G:THR196 3.3 8.6 1.0 C G:SER177 3.4 8.0 1.0 CG G:ASP201 3.4 7.9 1.0 CB G:THR196 3.6 8.1 1.0 CB G:SER177 3.6 7.7 1.0 CA G:SER177 3.6 7.3 1.0 C G:ILE199 3.7 9.4 1.0 OD2 G:ASP201 3.8 8.6 1.0 CA G:THR196 3.8 8.1 1.0 N G:ASP201 4.1 8.5 1.0 N G:PRO197 4.2 8.7 1.0 N G:THR196 4.3 7.7 1.0 CB G:ASP194 4.4 7.4 1.0 N G:ILE199 4.4 9.1 1.0 CA G:PRO197 4.4 8.5 1.0 CA G:ILE199 4.5 9.2 1.0 O G:ASP201 4.5 7.3 1.0 O G:HOH698 4.5 9.1 1.0 N G:VAL178 4.6 8.2 1.0 CB G:ASP201 4.6 8.4 1.0 CB G:ILE199 4.6 10.0 1.0 N G:PHE200 4.7 8.4 1.0 CB G:GLN203 4.7 8.1 1.0 CA G:ASP201 4.8 8.1 1.0 CG1 G:VAL178 4.8 9.0 1.0 CA G:PHE200 4.8 8.5 1.0 C G:ASP201 4.8 8.1 1.0 CG2 G:THR196 4.9 8.6 1.0 C G:PHE200 4.9 8.5 1.0 C G:PRO197 5.0 8.6 1.0

H.Son, H.Seo, L.T.M.Pham, S.H.Kang, K.-J.Kim, Y.H.Kim. Reinforced Helix-Loop Interaction of Lignin Peroxidase H8 of Phanerochaete Chrysosporium (LIPH8) For Improving Acid-pH Stability As Well As Thermostability To Be Published.