Iron in PDB 4w7k: Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant

All present enzymatic activity of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant:
1.11.1.19;

The structure of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant, PDB code: 4w7k 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)	33.63 / 1.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	183.950, 55.870, 104.000, 90.00, 118.26, 90.00
R / Rfree (%)	13.5 / 15.7

The binding sites of Iron atom in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant (pdb code 4w7k). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant, PDB code: 4w7k:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:6.5 occ:1.00 FE A:HEM501 0.0 6.5 1.0 NC A:HEM501 2.0 7.0 1.0 NA A:HEM501 2.1 7.4 1.0 ND A:HEM501 2.1 7.4 1.0 NB A:HEM501 2.1 8.2 1.0 NE2 A:HIS304 2.1 7.2 1.0 O A:HOH1338 2.3 28.6 1.0 C4C A:HEM501 3.1 6.9 1.0 C1A A:HEM501 3.1 7.7 1.0 CE1 A:HIS304 3.1 7.0 1.0 C1D A:HEM501 3.1 7.2 1.0 C4D A:HEM501 3.1 6.9 1.0 C1C A:HEM501 3.1 6.2 1.0 C4A A:HEM501 3.1 7.8 1.0 C4B A:HEM501 3.1 7.1 1.0 C1B A:HEM501 3.1 8.4 1.0 CD2 A:HIS304 3.1 7.2 1.0 HE1 A:HIS304 3.2 8.4 1.0 HD2 A:HIS304 3.3 8.6 1.0 CHD A:HEM501 3.4 7.3 1.0 CHA A:HEM501 3.4 7.5 1.0 CHB A:HEM501 3.4 8.4 1.0 CHC A:HEM501 3.5 7.3 1.0 O A:HOH1316 3.7 22.8 1.0 HH11 A:ARG332 3.8 11.1 1.0 O A:HOH1315 3.9 21.9 1.0 ND1 A:HIS304 4.2 7.1 1.0 CG A:HIS304 4.3 7.3 1.0 C3C A:HEM501 4.3 6.7 1.0 NH1 A:ARG332 4.3 9.2 1.0 C2A A:HEM501 4.3 7.3 1.0 C2C A:HEM501 4.3 6.9 1.0 C3A A:HEM501 4.3 7.7 1.0 C3B A:HEM501 4.3 7.6 1.0 C3D A:HEM501 4.3 7.6 1.0 C2B A:HEM501 4.3 7.8 1.0 C2D A:HEM501 4.3 7.5 1.0 HD2 A:ARG332 4.3 11.7 1.0 HH12 A:ARG332 4.5 11.1 1.0 HG1 A:THR308 4.5 10.4 1.0 HG21 A:THR308 4.6 11.6 1.0 HE2 A:PHE359 4.6 11.8 1.0 HD3 A:ARG332 4.6 11.7 1.0 HG21 A:ILE398 4.8 11.3 1.0 CD A:ARG332 4.9 9.7 1.0 HD1 A:HIS304 5.0 8.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:6.5 occ:1.00 FE B:HEM501 0.0 6.5 1.0 ND B:HEM501 2.0 6.4 1.0 NA B:HEM501 2.1 7.4 1.0 NB B:HEM501 2.1 8.2 1.0 NC B:HEM501 2.1 6.8 1.0 NE2 B:HIS304 2.1 7.1 1.0 O B:HOH1334 2.2 22.2 1.0 C4C B:HEM501 3.1 6.0 1.0 C4D B:HEM501 3.1 6.9 1.0 C4B B:HEM501 3.1 7.2 1.0 C1B B:HEM501 3.1 9.0 1.0 C1A B:HEM501 3.1 6.9 1.0 C4A B:HEM501 3.1 8.6 1.0 C1D B:HEM501 3.1 6.8 1.0 CE1 B:HIS304 3.1 7.2 1.0 C1C B:HEM501 3.1 6.8 1.0 CD2 B:HIS304 3.1 7.2 1.0 HE1 B:HIS304 3.2 8.6 1.0 HD2 B:HIS304 3.3 8.7 1.0 CHD B:HEM501 3.4 6.7 1.0 CHB B:HEM501 3.4 8.7 1.0 CHA B:HEM501 3.4 7.2 1.0 CHC B:HEM501 3.5 7.1 1.0 O B:HOH1333 3.7 25.9 1.0 HH11 B:ARG332 3.9 10.5 1.0 O B:HOH1332 4.0 24.9 1.0 ND1 B:HIS304 4.2 7.1 1.0 CG B:HIS304 4.3 6.7 1.0 C3C B:HEM501 4.3 6.7 1.0 C3B B:HEM501 4.3 7.8 1.0 NH1 B:ARG332 4.3 8.8 1.0 C2C B:HEM501 4.3 6.3 1.0 C2B B:HEM501 4.3 8.3 1.0 C2A B:HEM501 4.3 7.6 1.0 C3D B:HEM501 4.3 7.0 1.0 C3A B:HEM501 4.3 8.0 1.0 C2D B:HEM501 4.3 7.3 1.0 HD2 B:ARG332 4.4 10.0 1.0 HH12 B:ARG332 4.5 10.5 1.0 HG1 B:THR308 4.6 10.4 1.0 HE2 B:PHE359 4.6 12.5 1.0 HG21 B:THR308 4.6 12.1 1.0 HD3 B:ARG332 4.6 10.0 1.0 HG21 B:ILE398 4.7 11.7 1.0 CD B:ARG332 4.9 8.3 1.0 HD1 B:HIS304 5.0 8.5 1.0

D.Linde, R.Pogni, M.Canellas, F.Lucas, V.Guallar, M.C.Baratto, A.Sinicropi, V.Saez-Jimenez, C.Coscolin, A.Romero, F.J.Medrano, F.J.Ruiz-Duenas, A.T.Martinez. Catalytic Surface Radical in Dye-Decolorizing Peroxidase: A Computational, Spectroscopic and Site-Directed Mutagenesis Study. Biochem.J. V. 466 253 2015.
ISSN: ESSN 1470-8728
PubMed: 25495127
DOI: 10.1042/BJ20141211