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Iron in PDB 4w7n: Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S and W377S Double Mutant

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

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

Protein crystallography data

The structure of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S and W377S Double Mutant, PDB code: 4w7n 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) 42.99 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.470, 55.900, 103.900, 90.00, 118.17, 90.00
R / Rfree (%) 14.4 / 18.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S and W377S Double Mutant (pdb code 4w7n). 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 and W377S Double Mutant, PDB code: 4w7n:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4w7n

Go back to Iron Binding Sites List in 4w7n
Iron binding site 1 out of 2 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S and W377S Double 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 and W377S Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:9.7
occ:1.00
FE A:HEM501 0.0 9.7 1.0
NA A:HEM501 2.0 9.8 1.0
NC A:HEM501 2.1 9.6 1.0
NB A:HEM501 2.1 9.7 1.0
ND A:HEM501 2.1 10.8 1.0
NE2 A:HIS304 2.1 9.8 1.0
C4C A:HEM501 3.1 8.0 1.0
C4A A:HEM501 3.1 11.2 1.0
CE1 A:HIS304 3.1 10.9 1.0
C1A A:HEM501 3.1 9.9 1.0
C1B A:HEM501 3.1 11.2 1.0
C1C A:HEM501 3.1 7.2 1.0
C1D A:HEM501 3.1 8.5 1.0
C4B A:HEM501 3.1 10.3 1.0
C4D A:HEM501 3.1 8.0 1.0
CD2 A:HIS304 3.2 11.3 1.0
HE1 A:HIS304 3.2 13.1 1.0
HD2 A:HIS304 3.3 13.5 1.0
CHD A:HEM501 3.4 9.3 1.0
CHB A:HEM501 3.4 11.8 1.0
CHA A:HEM501 3.5 10.0 1.0
CHC A:HEM501 3.5 8.3 1.0
HH11 A:ARG332 3.8 13.3 1.0
O A:HOH1132 3.9 21.7 1.0
ND1 A:HIS304 4.2 9.8 1.0
HD2 A:ARG332 4.2 15.4 1.0
NH1 A:ARG332 4.3 11.1 1.0
C3C A:HEM501 4.3 8.3 1.0
C3A A:HEM501 4.3 8.6 1.0
CG A:HIS304 4.3 9.7 1.0
C2A A:HEM501 4.3 9.6 1.0
C2C A:HEM501 4.3 9.0 1.0
C2B A:HEM501 4.3 10.7 1.0
C3B A:HEM501 4.3 10.8 1.0
C2D A:HEM501 4.3 10.2 1.0
C3D A:HEM501 4.3 9.4 1.0
HHD A:HEM501 4.4 11.2 1.0
HHB A:HEM501 4.4 14.2 1.0
HHA A:HEM501 4.4 12.0 1.0
HHC A:HEM501 4.4 10.0 1.0
HG21 A:THR308 4.4 16.3 1.0
HH12 A:ARG332 4.5 13.3 1.0
HE1 A:PHE359 4.5 16.0 1.0
HG1 A:THR308 4.6 15.2 1.0
HD3 A:ARG332 4.6 15.4 1.0
CD A:ARG332 4.8 12.8 1.0
HG21 A:ILE398 4.9 14.7 1.0
HD1 A:HIS304 5.0 11.8 1.0

Iron binding site 2 out of 2 in 4w7n

Go back to Iron Binding Sites List in 4w7n
Iron binding site 2 out of 2 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. Y147S and W377S Double 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 and W377S Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:9.7
occ:1.00
FE B:HEM501 0.0 9.7 1.0
NB B:HEM501 2.0 11.5 1.0
NA B:HEM501 2.1 10.8 1.0
NC B:HEM501 2.1 9.7 1.0
ND B:HEM501 2.1 10.1 1.0
NE2 B:HIS304 2.1 10.6 1.0
C4C B:HEM501 3.1 7.3 1.0
C4B B:HEM501 3.1 11.0 1.0
C1B B:HEM501 3.1 12.7 1.0
C1D B:HEM501 3.1 8.7 1.0
C4A B:HEM501 3.1 11.9 1.0
C1A B:HEM501 3.1 8.3 1.0
C4D B:HEM501 3.1 9.0 1.0
C1C B:HEM501 3.1 8.8 1.0
CE1 B:HIS304 3.1 11.0 1.0
CD2 B:HIS304 3.1 10.7 1.0
HE1 B:HIS304 3.3 13.2 1.0
HD2 B:HIS304 3.3 12.9 1.0
CHD B:HEM501 3.4 7.7 1.0
CHA B:HEM501 3.4 9.4 1.0
CHB B:HEM501 3.4 13.8 1.0
CHC B:HEM501 3.4 10.8 1.0
HH11 B:ARG332 3.8 13.1 1.0
O B:HOH850 4.0 24.3 1.0
ND1 B:HIS304 4.2 10.4 1.0
HD2 B:ARG332 4.3 10.7 1.0
NH1 B:ARG332 4.3 10.9 1.0
C3C B:HEM501 4.3 9.2 1.0
C3B B:HEM501 4.3 12.1 1.0
CG B:HIS304 4.3 10.3 1.0
C2B B:HEM501 4.3 13.8 1.0
C3A B:HEM501 4.3 12.1 1.0
C2C B:HEM501 4.3 9.3 1.0
C2A B:HEM501 4.3 11.7 1.0
C2D B:HEM501 4.3 9.4 1.0
C3D B:HEM501 4.3 10.3 1.0
HHD B:HEM501 4.4 9.2 1.0
HHB B:HEM501 4.4 16.6 1.0
HHC B:HEM501 4.4 12.9 1.0
HHA B:HEM501 4.4 11.3 1.0
HG21 B:THR308 4.4 15.4 1.0
HH12 B:ARG332 4.5 13.1 1.0
HE1 B:PHE359 4.5 15.5 1.0
HD3 B:ARG332 4.6 10.7 1.0
HG1 B:THR308 4.6 15.4 1.0
CD B:ARG332 4.8 8.9 1.0
HG21 B:ILE398 4.8 18.8 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 14:18:55 2024

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