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Atomistry » Copper » PDB 4hhw-4mai » 4j6v | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Copper » PDB 4hhw-4mai » 4j6v » |
Copper in PDB 4j6v: Crystal Structure of Tyrosinase From Bacillus Megaterium N205D MutantEnzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium N205D Mutant
All present enzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium N205D Mutant:
1.14.18.1; Protein crystallography data
The structure of Crystal Structure of Tyrosinase From Bacillus Megaterium N205D Mutant, PDB code: 4j6v
was solved by
M.Kanteev,
M.Goldfeder,
N.Adir,
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 N205D Mutant
(pdb code 4j6v). 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 N205D Mutant, PDB code: 4j6v: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 4j6vGo back to Copper Binding Sites List in 4j6v
Copper binding site 1 out
of 2 in the Crystal Structure of Tyrosinase From Bacillus Megaterium N205D Mutant
Mono view Stereo pair view
Copper binding site 2 out of 2 in 4j6vGo back to Copper Binding Sites List in 4j6v
Copper binding site 2 out
of 2 in the Crystal Structure of Tyrosinase From Bacillus Megaterium N205D Mutant
Mono view Stereo pair view
Reference:
M.Kanteev,
M.Goldfeder,
M.Chojnacki,
N.Adir,
A.Fishman.
The Mechanism of Copper Uptake By Tyrosinase From Bacillus Megaterium. J.Biol.Inorg.Chem. V. 18 895 2013.
Page generated: Sun Dec 13 11:14:50 2020
ISSN: ISSN 0949-8257 PubMed: 24061559 DOI: 10.1007/S00775-013-1034-0 |
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