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Atomistry » Zinc » PDB 3lt8-3m1j » 3lzn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3lt8-3m1j » 3lzn » |
Zinc in PDB 3lzn: Crystal Structure Analysis of the Apo P19 Protein From Campylobacter Jejuni at 1.59 A at pH 9Protein crystallography data
The structure of Crystal Structure Analysis of the Apo P19 Protein From Campylobacter Jejuni at 1.59 A at pH 9, PDB code: 3lzn
was solved by
T.I.Doukov,
A.C.K.Chan,
M.Scofield,
A.B.Ramin,
S.A.L.Tom-Yew,
M.E.P.Murphy,
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 Crystal Structure Analysis of the Apo P19 Protein From Campylobacter Jejuni at 1.59 A at pH 9
(pdb code 3lzn). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure Analysis of the Apo P19 Protein From Campylobacter Jejuni at 1.59 A at pH 9, PDB code: 3lzn: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3lznGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Crystal Structure Analysis of the Apo P19 Protein From Campylobacter Jejuni at 1.59 A at pH 9
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 3lznGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Crystal Structure Analysis of the Apo P19 Protein From Campylobacter Jejuni at 1.59 A at pH 9
![]() Mono view ![]() Stereo pair view
Reference:
A.C.Chan,
T.I.Doukov,
M.Scofield,
S.A.Tom-Yew,
A.B.Ramin,
J.K.Mackichan,
E.C.Gaynor,
M.E.Murphy.
Structure and Function of P19, A High-Affinity Iron Transporter of the Human Pathogen Campylobacter Jejuni. J.Mol.Biol. V. 401 590 2010.
Page generated: Wed Dec 16 04:33:32 2020
ISSN: ISSN 0022-2836 PubMed: 20600116 DOI: 10.1016/J.JMB.2010.06.038 |
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