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Atomistry » Zinc » PDB 3ciz-3cyu » 3cx3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3ciz-3cyu » 3cx3 » |
Zinc in PDB 3cx3: Crystal Structure Analysis of the Streptococcus Pneumoniae Adcaii ProteinProtein crystallography data
The structure of Crystal Structure Analysis of the Streptococcus Pneumoniae Adcaii Protein, PDB code: 3cx3
was solved by
E.Loisel,
C.Durmort,
L.Jacquamet,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3cx3:
The structure of Crystal Structure Analysis of the Streptococcus Pneumoniae Adcaii Protein also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure Analysis of the Streptococcus Pneumoniae Adcaii Protein
(pdb code 3cx3). 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 Streptococcus Pneumoniae Adcaii Protein, PDB code: 3cx3: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3cx3Go back to Zinc Binding Sites List in 3cx3
Zinc binding site 1 out
of 2 in the Crystal Structure Analysis of the Streptococcus Pneumoniae Adcaii Protein
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 3cx3Go back to Zinc Binding Sites List in 3cx3
Zinc binding site 2 out
of 2 in the Crystal Structure Analysis of the Streptococcus Pneumoniae Adcaii Protein
Mono view Stereo pair view
Reference:
E.Loisel,
L.Jacquamet,
L.Serre,
C.Bauvois,
J.L.Ferrer,
T.Vernet,
A.M.Di Guilmi,
C.Durmort.
Adcaii, A New Pneumococcal Zn-Binding Protein Homologous with Abc Transporters: Biochemical and Structural Analysis. J.Mol.Biol. V. 381 594 2008.
Page generated: Wed Dec 16 04:11:29 2020
ISSN: ISSN 0022-2836 PubMed: 18632116 DOI: 10.1016/J.JMB.2008.05.068 |
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