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Iron in PDB 4w7o: Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple Mutant

Enzymatic activity of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple Mutant

All present enzymatic activity of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple Mutant:
1.11.1.19;

Protein crystallography data

The structure of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple Mutant, PDB code: 4w7o 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) 46.31 / 1.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 104.370, 56.095, 82.041, 90.00, 96.90, 90.00
R / Rfree (%) 14.1 / 15.3

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple Mutant (pdb code 4w7o). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple Mutant, PDB code: 4w7o:

Iron binding site 1 out of 1 in 4w7o

Go back to Iron Binding Sites List in 4w7o
Iron binding site 1 out of 1 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. G169L, Y147S and W377S Triple 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. G169L, Y147S and W377S Triple Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:8.8
occ:1.00
 FE A:HEM501 0.0 8.8 1.0
NC A:HEM501 2.0 8.9 1.0
ND A:HEM501 2.1 8.3 1.0
NA A:HEM501 2.1 9.2 1.0
NB A:HEM501 2.1 10.1 1.0
NE2 A:HIS304 2.1 9.3 1.0
C4C A:HEM501 3.0 8.6 1.0
C4A A:HEM501 3.1 10.1 1.0
C1D A:HEM501 3.1 9.0 1.0
C1C A:HEM501 3.1 8.8 1.0
C1A A:HEM501 3.1 8.9 1.0
C4B A:HEM501 3.1 10.3 1.0
CE1 A:HIS304 3.1 9.0 1.0
C4D A:HEM501 3.1 8.5 1.0
C1B A:HEM501 3.1 11.6 1.0
CD2 A:HIS304 3.1 8.9 1.0
HE1 A:HIS304 3.3 10.8 1.0
HD2 A:HIS304 3.3 10.7 1.0
CHD A:HEM501 3.4 8.9 1.0
CHA A:HEM501 3.4 8.4 1.0
CHB A:HEM501 3.4 10.6 1.0
CHC A:HEM501 3.4 9.2 1.0
O A:HOH921 3.6 25.9 1.0
HH11 A:ARG332 3.7 13.2 1.0
NH1 A:ARG332 4.2 11.0 1.0
ND1 A:HIS304 4.2 9.3 1.0
CG A:HIS304 4.3 9.5 1.0
C3C A:HEM501 4.3 9.3 1.0
C2C A:HEM501 4.3 9.3 1.0
C3A A:HEM501 4.3 9.7 1.0
C2A A:HEM501 4.3 9.4 1.0
C3B A:HEM501 4.3 10.8 1.0
C2B A:HEM501 4.3 11.5 1.0
C3D A:HEM501 4.3 9.5 1.0
C2D A:HEM501 4.3 9.7 1.0
HH12 A:ARG332 4.3 13.2 1.0
HD2 A:ARG332 4.4 12.6 1.0
HHD A:HEM501 4.4 10.7 1.0
HHA A:HEM501 4.4 10.1 1.0
HHB A:HEM501 4.4 12.8 1.0
HHC A:HEM501 4.4 11.0 1.0
HG21 A:THR308 4.4 13.7 1.0
HE2 A:PHE359 4.5 15.1 1.0
HG1 A:THR308 4.6 13.1 1.0
HD3 A:ARG332 4.6 12.6 1.0
HG21 A:ILE398 4.9 14.9 1.0
CD A:ARG332 4.9 10.5 1.0
CZ A:ARG332 5.0 10.4 1.0
HD1 A:HIS304 5.0 11.2 1.0

Reference:

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
Page generated: Mon Aug 5 14:19:03 2024

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