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Atomistry » Manganese » PDB 2feu-2hr6 » 2hbl » |
Manganese in PDB 2hbl: Structure of the Yeast Nuclear Exosome Component, RRP6P, Reveals An Interplay Between the Active Site and the Hrdc Domain; Protein in Complex with Mn, Zn, and AmpProtein crystallography data
The structure of Structure of the Yeast Nuclear Exosome Component, RRP6P, Reveals An Interplay Between the Active Site and the Hrdc Domain; Protein in Complex with Mn, Zn, and Amp, PDB code: 2hbl
was solved by
S.F.Midtgaard,
J.Assenholt,
A.T.Jonstrup,
L.B.Van,
T.H.Jensen,
D.E.Brodersen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2hbl:
The structure of Structure of the Yeast Nuclear Exosome Component, RRP6P, Reveals An Interplay Between the Active Site and the Hrdc Domain; Protein in Complex with Mn, Zn, and Amp also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of the Yeast Nuclear Exosome Component, RRP6P, Reveals An Interplay Between the Active Site and the Hrdc Domain; Protein in Complex with Mn, Zn, and Amp
(pdb code 2hbl). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of the Yeast Nuclear Exosome Component, RRP6P, Reveals An Interplay Between the Active Site and the Hrdc Domain; Protein in Complex with Mn, Zn, and Amp, PDB code: 2hbl: Manganese binding site 1 out of 1 in 2hblGo back to![]() ![]()
Manganese binding site 1 out
of 1 in the Structure of the Yeast Nuclear Exosome Component, RRP6P, Reveals An Interplay Between the Active Site and the Hrdc Domain; Protein in Complex with Mn, Zn, and Amp
![]() Mono view ![]() Stereo pair view
Reference:
S.F.Midtgaard,
J.Assenholt,
A.T.Jonstrup,
L.B.Van,
T.H.Jensen,
D.E.Brodersen.
Structure of the Nuclear Exosome Component RRP6P Reveals An Interplay Between the Active Site and the Hrdc Domain. Proc.Natl.Acad.Sci.Usa V. 103 11898 2006.
Page generated: Sat Oct 5 14:17:03 2024
ISSN: ISSN 0027-8424 PubMed: 16882719 DOI: 10.1073/PNAS.0604731103 |
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