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Atomistry » Zinc » PDB 1nvf-1oi0 » 1oek | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1nvf-1oi0 » 1oek » |
Zinc in PDB 1oek: Yoda From Escherichia Coli Crystallised with Zinc IonsProtein crystallography data
The structure of Yoda From Escherichia Coli Crystallised with Zinc Ions, PDB code: 1oek
was solved by
G.David,
K.Blondeau,
M.Renouard,
S.Penel,
A.Lewit-Bentley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Yoda From Escherichia Coli Crystallised with Zinc Ions
(pdb code 1oek). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Yoda From Escherichia Coli Crystallised with Zinc Ions, PDB code: 1oek: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 1oekGo back to![]() ![]()
Zinc binding site 1 out
of 4 in the Yoda From Escherichia Coli Crystallised with Zinc Ions
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 4 in 1oekGo back to![]() ![]()
Zinc binding site 2 out
of 4 in the Yoda From Escherichia Coli Crystallised with Zinc Ions
![]() Mono view ![]() Stereo pair view
Zinc binding site 3 out of 4 in 1oekGo back to![]() ![]()
Zinc binding site 3 out
of 4 in the Yoda From Escherichia Coli Crystallised with Zinc Ions
![]() Mono view ![]() Stereo pair view
Zinc binding site 4 out of 4 in 1oekGo back to![]() ![]()
Zinc binding site 4 out
of 4 in the Yoda From Escherichia Coli Crystallised with Zinc Ions
![]() Mono view ![]() Stereo pair view
Reference:
G.David,
K.Blondeau,
M.Schiltz,
S.Penel,
A.Lewit-Bentley.
Yoda From Escherichia Coli Is A Metal-Binding, Lipocalin-Like Protein J.Biol.Chem. V. 278 43728 2003.
Page generated: Wed Oct 16 17:29:55 2024
ISSN: ISSN 0021-9258 PubMed: 12909634 DOI: 10.1074/JBC.M304484200 |
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