Calcium in PDB 2w23: Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp)

All present enzymatic activity of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp):
1.11.1.16;

The structure of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp), PDB code: 2w23 was solved by F.J.Ruiz-Duenas, R.Pogni, M.Morales, S.Giansanti, M.J.Mate, A.Romero, M.J.Martinez, R.Basosi, A.T.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.01 / 1.94
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	96.740, 96.740, 98.190, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 17.5

The structure of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Calcium atom in the Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) (pdb code 2w23). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp), PDB code: 2w23:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1317 b:8.0 occ:1.00 O A:HOH2065 2.4 5.0 1.0 OD1 A:ASP48 2.4 5.4 1.0 OG A:SER64 2.5 5.9 1.0 O A:GLY60 2.5 6.7 1.0 OD1 A:ASP62 2.5 7.4 1.0 O A:HOH2087 2.5 4.8 1.0 O A:ASP48 2.6 6.0 1.0 CG A:ASP48 3.4 7.5 1.0 C A:ASP48 3.4 6.5 1.0 CG A:ASP62 3.6 9.0 1.0 CB A:SER64 3.6 7.3 1.0 C A:GLY60 3.6 6.7 1.0 CA A:ASP48 3.8 6.6 1.0 N A:SER64 3.9 8.0 1.0 OD2 A:ASP62 4.1 9.8 1.0 O A:HOH2074 4.1 6.9 1.0 N A:ASP62 4.2 7.6 1.0 CB A:ASP48 4.2 7.0 1.0 OD2 A:ASP48 4.2 8.1 1.0 CA A:SER64 4.3 7.8 1.0 CA A:GLY60 4.3 6.8 1.0 N A:GLY60 4.4 7.0 1.0 N A:ILE65 4.4 7.9 1.0 O A:GLY51 4.5 8.1 1.0 OE2 A:GLU72 4.5 9.6 1.0 N A:GLY63 4.6 7.4 1.0 N A:ALA49 4.6 5.9 1.0 OE1 A:GLU72 4.7 9.9 1.0 N A:ALA61 4.7 7.4 1.0 CB A:ASP62 4.7 7.7 1.0 C A:SER64 4.8 7.7 1.0 CA A:ASP62 4.8 8.1 1.0 CA A:GLY51 4.8 8.1 1.0 CA A:ALA61 4.9 7.3 1.0 N A:GLY51 5.0 7.9 1.0 O A:HIS47 5.0 7.6 1.0 C A:GLY59 5.0 6.9 1.0 CA A:ALA49 5.0 6.5 1.0 C A:ASP62 5.0 8.0 1.0

Calcium binding site 2 out of 2 in the Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1318 b:8.0 occ:1.00 O A:VAL192 2.4 5.8 1.0 O A:SER170 2.4 4.6 1.0 O A:THR189 2.4 7.2 1.0 OD2 A:ASP187 2.4 5.8 1.0 OG A:SER170 2.5 6.2 1.0 OD1 A:ASP194 2.5 5.0 1.0 OG1 A:THR189 2.6 6.6 1.0 OD1 A:ASP187 2.7 6.2 1.0 CG A:ASP187 3.0 6.0 1.0 C A:THR189 3.3 6.7 1.0 C A:SER170 3.3 4.8 1.0 CG A:ASP194 3.4 6.9 1.0 CB A:THR189 3.6 6.8 1.0 CB A:SER170 3.6 5.5 1.0 C A:VAL192 3.6 7.0 1.0 CA A:SER170 3.7 5.5 1.0 OD2 A:ASP194 3.8 5.9 1.0 CA A:THR189 3.8 6.8 1.0 N A:ASP194 4.1 6.5 1.0 N A:THR189 4.2 7.0 1.0 N A:PRO190 4.3 6.6 1.0 N A:VAL192 4.4 8.4 1.0 CA A:VAL192 4.4 7.5 1.0 CB A:VAL192 4.5 7.6 1.0 O A:ASP194 4.5 6.6 1.0 CB A:ASP187 4.5 6.1 1.0 O A:HOH2218 4.5 6.7 1.0 CA A:PRO190 4.6 6.9 1.0 N A:ILE171 4.6 4.7 1.0 N A:PHE193 4.6 6.5 1.0 CB A:ASP194 4.6 6.9 1.0 CB A:GLN196 4.6 7.3 1.0 CA A:ASP194 4.7 6.9 1.0 CA A:PHE193 4.8 6.4 1.0 CG2 A:ILE171 4.8 4.1 1.0 C A:ASP194 4.9 7.1 1.0 C A:PHE193 4.9 6.5 1.0 CG2 A:THR189 4.9 6.8 1.0 C A:PRO190 5.0 7.3 1.0

F.J.Ruiz-Duenas, R.Pogni, M.Morales, S.Giansanti, M.J.Mate, A.Romero, M.J.Martinez, R.Basosi, A.T.Martinez. Protein Radicals in Fungal Versatile Peroxidase: Catalytic Tryptophan Radical in Both Compound I and Compound II and Studies on W164Y, W164H, and W164S Variants. J.Biol.Chem. V. 284 7986 2009.
ISSN: ISSN 0021-9258
PubMed: 19158088
DOI: 10.1074/JBC.M808069200