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Iron in PDB 2vka: Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase

Enzymatic activity of Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase

All present enzymatic activity of Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase:
1.11.1.16;

Protein crystallography data

The structure of Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase, PDB code: 2vka was solved by F.J.Ruiz-Duenas, M.Morales, M.J.Mate, A.Romero, M.J.Martinez, A.Smith, A.T.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.12 / 2.00
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 96.290, 96.290, 98.530, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 18.5

Other elements in 2vka:

The structure of Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase (pdb code 2vka). 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 Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase, PDB code: 2vka:

Iron binding site 1 out of 1 in 2vka

Go back to Iron Binding Sites List in 2vka
Iron binding site 1 out of 1 in the Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1320

b:2.8
occ:1.00
 FE A:HEM1320 0.0 2.8 1.0
NA A:HEM1320 2.0 2.0 1.0
NC A:HEM1320 2.1 2.0 1.0
NB A:HEM1320 2.1 2.2 1.0
NE2 A:HIS169 2.2 9.7 1.0
ND A:HEM1320 2.2 2.4 1.0
O A:HOH2071 2.7 13.8 1.0
C4A A:HEM1320 3.1 2.6 1.0
C1C A:HEM1320 3.1 2.0 1.0
C1A A:HEM1320 3.1 2.0 1.0
C4C A:HEM1320 3.1 2.9 1.0
CE1 A:HIS169 3.1 8.1 1.0
C4B A:HEM1320 3.1 2.0 1.0
C1D A:HEM1320 3.1 2.0 1.0
C1B A:HEM1320 3.1 2.0 1.0
C4D A:HEM1320 3.2 2.4 1.0
CD2 A:HIS169 3.2 8.1 1.0
CHD A:HEM1320 3.4 2.0 1.0
CHC A:HEM1320 3.4 2.0 1.0
CHB A:HEM1320 3.5 2.0 1.0
CHA A:HEM1320 3.5 2.0 1.0
ND1 A:HIS169 4.2 8.7 1.0
C3A A:HEM1320 4.3 2.1 1.0
C2A A:HEM1320 4.3 2.2 1.0
C2C A:HEM1320 4.3 2.0 1.0
CG A:HIS169 4.3 8.7 1.0
C2D A:HEM1320 4.3 2.0 1.0
C3B A:HEM1320 4.3 2.8 1.0
C2B A:HEM1320 4.3 2.0 1.0
C3C A:HEM1320 4.3 2.0 1.0
C3D A:HEM1320 4.3 2.0 1.0
O A:HOH2210 4.4 29.7 1.0
O A:HOH2063 4.8 11.7 1.0
CE2 A:PHE186 5.0 7.9 1.0

Reference:

F.J.Ruiz-Duenas, M.Morales, M.J.Mate, A.Romero, M.J.Martinez, A.Smith, A.T.Martinez. Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus Eryngii Versatile Peroxidase Biochemistry V. 47 1685 2008.
ISSN: ISSN 0006-2960
PubMed: 18201105
DOI: 10.1021/BI7020298
Page generated: Sun Aug 4 02:38:54 2024

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