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Atomistry » Manganese » PDB 2feu-2hr6 » 2hbm » |
Manganese in PDB 2hbm: 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 UmpProtein 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 Ump, PDB code: 2hbm
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 2hbm:
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 Ump 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 Ump
(pdb code 2hbm). 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 Ump, PDB code: 2hbm: Manganese binding site 1 out of 1 in 2hbmGo back to Manganese Binding Sites List in 2hbm
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 Ump
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: Tue Dec 15 04:02:27 2020
ISSN: ISSN 0027-8424 PubMed: 16882719 DOI: 10.1073/PNAS.0604731103 |
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