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Iron in PDB 5abq: Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R.

Enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R.

All present enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R.:
1.11.1.16;

Protein crystallography data

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R., PDB code: 5abq 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) 43.909 / 2.29
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.915, 68.763, 87.818, 90.00, 90.00, 90.00
R / Rfree (%) 24.8 / 30.04

Other elements in 5abq:

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R. also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R. (pdb code 5abq). 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 Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R., PDB code: 5abq:

Iron binding site 1 out of 1 in 5abq

Go back to Iron Binding Sites List in 5abq
Iron binding site 1 out of 1 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi-Ss. Mutated Residues T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K and A314R. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:37.7
occ:1.00
 FE A:HEM500 0.0 37.7 1.0
NA A:HEM500 2.1 31.7 1.0
NC A:HEM500 2.1 30.4 1.0
NB A:HEM500 2.1 34.0 1.0
ND A:HEM500 2.1 34.4 1.0
NE2 A:HIS169 2.7 53.0 1.0
C1C A:HEM500 3.1 31.7 1.0
C1A A:HEM500 3.1 34.2 1.0
C4A A:HEM500 3.1 32.4 1.0
C1D A:HEM500 3.1 34.0 1.0
C4C A:HEM500 3.1 32.2 1.0
C1B A:HEM500 3.1 33.4 1.0
C4D A:HEM500 3.1 34.3 1.0
C4B A:HEM500 3.1 33.3 1.0
CHD A:HEM500 3.4 32.8 1.0
CHC A:HEM500 3.4 32.4 1.0
CHA A:HEM500 3.4 33.1 1.0
CHB A:HEM500 3.4 32.7 1.0
CD2 A:HIS169 3.5 52.6 1.0
CE1 A:HIS169 3.8 53.4 1.0
C2C A:HEM500 4.3 31.6 1.0
C3A A:HEM500 4.3 34.4 1.0
C2A A:HEM500 4.3 35.6 1.0
C3C A:HEM500 4.3 31.6 1.0
C2B A:HEM500 4.3 34.5 1.0
C2D A:HEM500 4.3 36.5 1.0
C3B A:HEM500 4.3 34.9 1.0
C3D A:HEM500 4.3 37.9 1.0
CG A:HIS169 4.7 53.7 1.0
ND1 A:HIS169 4.8 54.7 1.0
CG A:ARG43 5.0 38.2 1.0

Reference:

V.Saez-Jimenez, E.Fernendez-Fueyo, F.J.Medrano, A.Romero, A.T.Martinez, F.J.Ruiz-Duenas. Improving the pH-Stability of Versatile Peroxidase By Comparative Structural Analysis with A Naturally-Stable Manganese Peroxidase. Plos One V. 10 40984 2015.
ISSN: ISSN 1932-6203
PubMed: 26496708
DOI: 10.1371/JOURNAL.PONE.0140984
Page generated: Tue Aug 5 18:50:16 2025

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