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Iron in PDB 4w7m: Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. W377S Mutant

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

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

Protein crystallography data

The structure of Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. W377S Mutant, PDB code: 4w7m 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) 41.25 / 1.15
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.960, 56.170, 104.120, 90.00, 118.04, 90.00
R / Rfree (%) 13.1 / 15

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. W377S Mutant (pdb code 4w7m). 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. W377S Mutant, PDB code: 4w7m:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4w7m

Go back to Iron Binding Sites List in 4w7m
Iron binding site 1 out of 2 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. W377S 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. W377S Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:7.1
occ:1.00
FE A:HEM501 0.0 7.1 1.0
NB A:HEM501 2.0 9.6 1.0
ND A:HEM501 2.1 7.8 1.0
NC A:HEM501 2.1 7.1 1.0
NA A:HEM501 2.1 7.6 1.0
NE2 A:HIS304 2.1 6.7 1.0
O A:HOH1281 2.2 29.9 1.0
C4D A:HEM501 3.1 7.9 1.0
C1B A:HEM501 3.1 9.2 1.0
C4B A:HEM501 3.1 8.1 1.0
C1D A:HEM501 3.1 8.2 1.0
C4C A:HEM501 3.1 7.9 1.0
C1C A:HEM501 3.1 8.1 1.0
CE1 A:HIS304 3.1 7.4 1.0
C1A A:HEM501 3.1 8.4 1.0
CD2 A:HIS304 3.1 7.5 1.0
C4A A:HEM501 3.1 9.6 1.0
HE1 A:HIS304 3.3 8.8 1.0
HD2 A:HIS304 3.3 9.0 1.0
CHA A:HEM501 3.4 8.7 1.0
CHC A:HEM501 3.4 8.8 1.0
CHD A:HEM501 3.4 7.8 1.0
CHB A:HEM501 3.5 10.7 1.0
HH11 A:ARG332 3.9 11.6 1.0
O A:HOH1282 3.9 29.9 1.0
ND1 A:HIS304 4.2 7.7 1.0
CG A:HIS304 4.2 7.1 1.0
C2B A:HEM501 4.3 8.8 1.0
C3B A:HEM501 4.3 8.6 1.0
C3C A:HEM501 4.3 7.8 1.0
C3D A:HEM501 4.3 8.8 1.0
C2D A:HEM501 4.3 8.4 1.0
C2C A:HEM501 4.3 8.2 1.0
NH1 A:ARG332 4.3 9.7 1.0
C2A A:HEM501 4.3 8.8 1.0
C3A A:HEM501 4.3 9.3 1.0
HD2 A:ARG332 4.4 11.5 1.0
HG21 A:THR308 4.4 11.7 1.0
HH12 A:ARG332 4.5 11.6 1.0
HG1 A:THR308 4.5 11.3 1.0
HE2 A:PHE359 4.6 11.7 1.0
HD3 A:ARG332 4.6 11.5 1.0
HG21 A:ILE398 4.9 11.6 1.0
CD A:ARG332 4.9 9.6 1.0
HD1 A:HIS304 5.0 9.2 1.0

Iron binding site 2 out of 2 in 4w7m

Go back to Iron Binding Sites List in 4w7m
Iron binding site 2 out of 2 in the Crystal Structure of A Decolorizing Peroxidase (Dyp) From Auricularia Auricula-Judae. W377S 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. W377S Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:7.0
occ:1.00
FE B:HEM501 0.0 7.0 1.0
ND B:HEM501 2.0 7.0 1.0
NB B:HEM501 2.0 9.6 1.0
NC B:HEM501 2.1 6.8 1.0
NA B:HEM501 2.1 7.6 1.0
NE2 B:HIS304 2.1 6.8 1.0
O B:HOH1262 2.2 29.9 1.0
C4D B:HEM501 3.1 7.6 1.0
C1D B:HEM501 3.1 7.8 1.0
C1B B:HEM501 3.1 9.2 1.0
C4B B:HEM501 3.1 8.2 1.0
CE1 B:HIS304 3.1 7.9 1.0
C1C B:HEM501 3.1 8.2 1.0
C4C B:HEM501 3.1 8.2 1.0
C1A B:HEM501 3.1 8.4 1.0
C4A B:HEM501 3.1 10.1 1.0
CD2 B:HIS304 3.1 7.1 1.0
HE1 B:HIS304 3.2 9.5 1.0
HD2 B:HIS304 3.3 8.6 1.0
CHD B:HEM501 3.4 7.5 1.0
CHA B:HEM501 3.4 8.6 1.0
CHC B:HEM501 3.4 8.6 1.0
CHB B:HEM501 3.5 10.6 1.0
O B:HOH1263 3.6 29.9 1.0
HH11 B:ARG332 3.8 10.9 1.0
O B:HOH1162 4.0 22.4 1.0
ND1 B:HIS304 4.2 7.6 1.0
CG B:HIS304 4.3 7.2 1.0
C3B B:HEM501 4.3 8.4 1.0
C2B B:HEM501 4.3 8.7 1.0
C3C B:HEM501 4.3 8.2 1.0
C3D B:HEM501 4.3 8.7 1.0
C2C B:HEM501 4.3 7.9 1.0
NH1 B:ARG332 4.3 9.1 1.0
C2D B:HEM501 4.3 8.6 1.0
C3A B:HEM501 4.3 8.8 1.0
C2A B:HEM501 4.3 9.0 1.0
HD2 B:ARG332 4.3 10.8 1.0
HG21 B:THR308 4.4 11.7 1.0
HH12 B:ARG332 4.5 10.9 1.0
HG1 B:THR308 4.6 11.4 1.0
HE1 B:PHE359 4.6 12.6 1.0
HD3 B:ARG332 4.6 10.8 1.0
HG21 B:ILE398 4.8 12.5 1.0
CD B:ARG332 4.9 9.0 1.0
HD1 B:HIS304 5.0 9.2 1.0
HD13 B:ILE398 5.0 11.6 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: Sun Dec 13 15:50:37 2020

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