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Atomistry » Chlorine » PDB 5ltr-5lz4 » 5lww | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5ltr-5lz4 » 5lww » |
Chlorine in PDB 5lww: Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to ZincEnzymatic activity of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc
All present enzymatic activity of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc:
1.10.3.2; Protein crystallography data
The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc, PDB code: 5lww
was solved by
M.Ferraroni,
F.Briganti,
J.A.Tamayo-Ramos,
W.J.H.Van Berkel,
A.H.Westphal,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5lww:
The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc
(pdb code 5lww). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc, PDB code: 5lww: Chlorine binding site 1 out of 1 in 5lwwGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc
![]() Mono view ![]() Stereo pair view
Reference:
M.Ferraroni,
A.H.Westphal,
M.Borsari,
J.A.Tamayo-Ramos,
F.Briganti,
L.H.De Graaff,
W.J.H.Van Berkel.
Structure and Function of Aspergillus Niger Laccase Mcog Biocatalysis 2017.
Page generated: Sat Dec 12 12:04:35 2020
ISSN: ESSN 2353-1746 DOI: 10.1515/BOCA-2017-0001 |
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