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Atomistry » Iron » PDB 3h34-3hni » 3hjs » |
Iron in PDB 3hjs: Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-MethylcatecholEnzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol
All present enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol:
1.13.11.1; Protein crystallography data
The structure of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol, PDB code: 3hjs
was solved by
I.Matera,
M.Ferraroni,
F.Briganti,
A.Scozzafava,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3hjs:
The structure of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol
(pdb code 3hjs). 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 Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol, PDB code: 3hjs: Iron binding site 1 out of 1 in 3hjsGo back to Iron Binding Sites List in 3hjs
Iron binding site 1 out
of 1 in the Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 4-Methylcatechol
Mono view Stereo pair view
Reference:
I.Matera,
M.Ferraroni,
M.Kolomytseva,
L.Golovleva,
A.Scozzafava,
F.Briganti.
Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP: Quantitative Structure/Activity Relationship and the Crystal Structures of Native Enzyme and Catechols Adducts. J.Struct.Biol. V. 170 548 2010.
Page generated: Sun Dec 13 15:07:45 2020
ISSN: ISSN 1047-8477 PubMed: 20040374 DOI: 10.1016/J.JSB.2009.12.023 |
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