Iron in PDB 5fne: Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & G330R

Enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & G330R

All present enzymatic activity of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & G330R:
1.11.1.16;

Protein crystallography data

The structure of Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & G330R, PDB code: 5fne 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) 44.778 / 1.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 55.190, 104.200, 76.600, 90.00, 90.00, 90.00
R / Rfree (%) 19.24 / 22.92

Other elements in 5fne:

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

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & G330R (pdb code 5fne). 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 Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & G330R, PDB code: 5fne:

Iron binding site 1 out of 1 in 5fne

Go back to Iron Binding Sites List in 5fne
Iron binding site 1 out of 1 in the Crystal Structure of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37K, H39R & 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 Triple Mutant E37K, H39R & G330R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:14.8
occ:1.00
 FE A:HEM500 0.0 14.8 1.0
NC A:HEM500 2.0 12.1 1.0
NA A:HEM500 2.1 15.5 1.0
NB A:HEM500 2.1 16.2 1.0
ND A:HEM500 2.1 12.4 1.0
NE2 A:HIS169 2.2 10.9 1.0
O A:HOH2081 2.6 24.0 1.0
C1C A:HEM500 3.1 14.2 1.0
C1D A:HEM500 3.1 13.6 1.0
C4C A:HEM500 3.1 13.6 1.0
C4A A:HEM500 3.1 16.2 1.0
C1B A:HEM500 3.1 14.5 1.0
C4B A:HEM500 3.1 19.6 1.0
C1A A:HEM500 3.1 13.6 1.0
C4D A:HEM500 3.1 14.7 1.0
CE1 A:HIS169 3.1 13.0 1.0
CD2 A:HIS169 3.1 13.1 1.0
CHD A:HEM500 3.4 9.7 1.0
CHC A:HEM500 3.4 12.4 1.0
CHB A:HEM500 3.5 13.8 1.0
CHA A:HEM500 3.5 15.5 1.0
ND1 A:HIS169 4.3 14.1 1.0
C2C A:HEM500 4.3 13.5 1.0
C2D A:HEM500 4.3 11.1 1.0
C3C A:HEM500 4.3 15.2 1.0
CG A:HIS169 4.3 13.1 1.0
C3A A:HEM500 4.3 13.6 1.0
C3D A:HEM500 4.3 10.1 1.0
C2B A:HEM500 4.3 15.3 1.0
C2A A:HEM500 4.3 13.8 1.0
C3B A:HEM500 4.3 12.2 1.0
CE2 A:PHE186 5.0 13.9 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: Sun Dec 13 16:01:33 2020

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