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Atomistry » Zinc » PDB 3eb6-3ejt » 3egx » |
Zinc in PDB 3egx: Crystal Structure of the Mammalian Copii-Coat Protein SEC23A/24A Complexed with the Snare Protein SEC22B and Bound to the Transport Signal Sequence of the Snare Protein BET1Protein crystallography data
The structure of Crystal Structure of the Mammalian Copii-Coat Protein SEC23A/24A Complexed with the Snare Protein SEC22B and Bound to the Transport Signal Sequence of the Snare Protein BET1, PDB code: 3egx
was solved by
J.Goldberg,
J.D.Mancias,
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 of the Mammalian Copii-Coat Protein SEC23A/24A Complexed with the Snare Protein SEC22B and Bound to the Transport Signal Sequence of the Snare Protein BET1
(pdb code 3egx). 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 of the Mammalian Copii-Coat Protein SEC23A/24A Complexed with the Snare Protein SEC22B and Bound to the Transport Signal Sequence of the Snare Protein BET1, PDB code: 3egx: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3egxGo back to Zinc Binding Sites List in 3egx
Zinc binding site 1 out
of 2 in the Crystal Structure of the Mammalian Copii-Coat Protein SEC23A/24A Complexed with the Snare Protein SEC22B and Bound to the Transport Signal Sequence of the Snare Protein BET1
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 3egxGo back to Zinc Binding Sites List in 3egx
Zinc binding site 2 out
of 2 in the Crystal Structure of the Mammalian Copii-Coat Protein SEC23A/24A Complexed with the Snare Protein SEC22B and Bound to the Transport Signal Sequence of the Snare Protein BET1
Mono view Stereo pair view
Reference:
J.D.Mancias,
J.Goldberg.
Structural Basis of Cargo Membrane Protein Discrimination By the Human Copii Coat Machinery. Embo J. V. 27 2918 2008.
Page generated: Wed Dec 16 04:15:57 2020
ISSN: ISSN 0261-4189 PubMed: 18843296 DOI: 10.1038/EMBOJ.2008.208 |
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