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Iron in PDB 5fnb: Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R

Enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R

All present enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R:
1.11.1.16; 1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R, PDB code: 5fnb 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) 49.015 / 1.79
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.060, 106.010, 107.600, 90.00, 90.00, 90.00
R / Rfree (%) 18.51 / 21.94

Other elements in 5fnb:

The structure of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R (pdb code 5fnb). 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 Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R, PDB code: 5fnb:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5fnb

Go back to Iron Binding Sites List in 5fnb
Iron binding site 1 out of 2 in the Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R


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 Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:16.3
occ:1.00
 FE A:HEM500 0.0 16.3 1.0
NC A:HEM500 2.1 15.6 1.0
ND A:HEM500 2.1 12.6 1.0
NA A:HEM500 2.1 17.5 1.0
NB A:HEM500 2.1 15.0 1.0
NE2 A:HIS169 2.2 14.7 1.0
C1C A:HEM500 3.1 15.4 1.0
C4D A:HEM500 3.1 15.1 1.0
C1A A:HEM500 3.1 17.1 1.0
C1D A:HEM500 3.1 12.9 1.0
C4C A:HEM500 3.1 13.8 1.0
C4B A:HEM500 3.1 16.2 1.0
C4A A:HEM500 3.1 16.1 1.0
C1B A:HEM500 3.2 15.3 1.0
CE1 A:HIS169 3.2 15.8 1.0
CD2 A:HIS169 3.2 14.1 1.0
CHA A:HEM500 3.4 16.0 1.0
CHC A:HEM500 3.4 15.3 1.0
CHD A:HEM500 3.4 13.9 1.0
CHB A:HEM500 3.5 16.5 1.0
C3D A:HEM500 4.3 12.5 1.0
C2C A:HEM500 4.3 14.8 1.0
C2D A:HEM500 4.3 14.0 1.0
C2A A:HEM500 4.3 16.6 1.0
C3C A:HEM500 4.3 14.9 1.0
ND1 A:HIS169 4.3 15.0 1.0
C3A A:HEM500 4.3 16.4 1.0
C3B A:HEM500 4.4 15.9 1.0
C2B A:HEM500 4.4 17.8 1.0
CG A:HIS169 4.4 14.4 1.0
O A:HOH2063 4.5 26.4 1.0

Iron binding site 2 out of 2 in 5fnb

Go back to Iron Binding Sites List in 5fnb
Iron binding site 2 out of 2 in the Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R


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 Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37K, H39R, V160A, T184M, Q202L, D213A & G330R within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:18.1
occ:1.00
 FE B:HEM500 0.0 18.1 1.0
NC B:HEM500 2.0 15.4 1.0
NA B:HEM500 2.1 18.6 1.0
NB B:HEM500 2.1 15.9 1.0
ND B:HEM500 2.1 17.4 1.0
NE2 B:HIS169 2.3 17.4 1.0
O B:HOH2050 2.6 22.8 1.0
C4C B:HEM500 3.0 16.2 1.0
C4A B:HEM500 3.1 17.2 1.0
C1B B:HEM500 3.1 18.3 1.0
C1D B:HEM500 3.1 13.6 1.0
C1C B:HEM500 3.1 15.9 1.0
C1A B:HEM500 3.1 21.1 1.0
C4D B:HEM500 3.1 18.6 1.0
C4B B:HEM500 3.1 16.9 1.0
CE1 B:HIS169 3.2 15.9 1.0
CD2 B:HIS169 3.2 16.1 1.0
CHD B:HEM500 3.4 14.8 1.0
CHB B:HEM500 3.4 19.0 1.0
CHC B:HEM500 3.5 15.7 1.0
CHA B:HEM500 3.5 20.1 1.0
C3C B:HEM500 4.2 16.6 1.0
C2C B:HEM500 4.3 15.9 1.0
O B:HOH2043 4.3 25.7 1.0
C2B B:HEM500 4.3 17.4 1.0
C2D B:HEM500 4.3 16.6 1.0
C3A B:HEM500 4.3 18.7 1.0
C2A B:HEM500 4.3 18.5 1.0
C3D B:HEM500 4.3 17.4 1.0
ND1 B:HIS169 4.3 15.9 1.0
C3B B:HEM500 4.3 15.6 1.0
CG B:HIS169 4.4 15.6 1.0

Reference:

V.Saez-Jimenez, S.Acebes, E.Garcia-Ruiz, A.Romero, V.Guallar, M.Alcalde, F.J.Medrano, A.T.Martinez, F.J.Ruiz-Duenas. Unveiling the Basis of Alkaline Stability of An Evolved Versatile Peroxidase. Biochem.J. V. 473 1917 2016.
ISSN: ISSN 0264-6021
PubMed: 27118867
DOI: 10.1042/BCJ20160248
Page generated: Tue Aug 5 21:32:23 2025

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