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Calcium 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:
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 Binding Sites:
The binding sites of Calcium 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 Calcium atom.
In total 4 binding sites of Calcium where 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: Jump to Calcium binding site number: 1; 2; 3; 4; Calcium binding site 1 out of 4 in 5abqGo back to Calcium Binding Sites List in 5abq
Calcium binding site 1 out
of 4 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
Calcium binding site 2 out of 4 in 5abqGo back to Calcium Binding Sites List in 5abq
Calcium binding site 2 out
of 4 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
Calcium binding site 3 out of 4 in 5abqGo back to Calcium Binding Sites List in 5abq
Calcium binding site 3 out
of 4 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
Calcium binding site 4 out of 4 in 5abqGo back to Calcium Binding Sites List in 5abq
Calcium binding site 4 out
of 4 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
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.
Page generated: Sat Dec 12 05:17:16 2020
ISSN: ISSN 1932-6203 PubMed: 26496708 DOI: 10.1371/JOURNAL.PONE.0140984 |
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