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Atomistry » Copper » PDB 4b61-4e9t » 4d87 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Copper » PDB 4b61-4e9t » 4d87 » |
Copper in PDB 4d87: Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with SdsEnzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds
All present enzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds:
1.14.18.1; Protein crystallography data
The structure of Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds, PDB code: 4d87
was solved by
N.Adir,
M.Goldfeder,
A.Fishman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds
(pdb code 4d87). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds, PDB code: 4d87: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 4d87Go back to![]() ![]()
Copper binding site 1 out
of 2 in the Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds
![]() Mono view ![]() Stereo pair view
Copper binding site 2 out of 2 in 4d87Go back to![]() ![]()
Copper binding site 2 out
of 2 in the Crystal Structure of Tyrosinase From Bacillus Megaterium in Complex with Sds
![]() Mono view ![]() Stereo pair view
Reference:
M.Goldfeder,
M.Egozy,
V.Shuster Ben-Yosef,
N.Adir,
A.Fishman.
Changes in Tyrosinase Specificity By Ionic Liquids and Sodium Dodecyl Sulfate. Appl.Microbiol.Biotechnol. V. 97 1953 2013.
Page generated: Wed Jul 31 02:41:28 2024
ISSN: ISSN 0175-7598 PubMed: 22539021 DOI: 10.1007/S00253-012-4050-Z |
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