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Atomistry » Manganese » PDB 4k3v-4lt5 » 4ls9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 4k3v-4lt5 » 4ls9 » |
Manganese in PDB 4ls9: Structure of Mycobacterial Nrna Homolog Reveals Multifunctional Nuclease ActivitiesProtein crystallography data
The structure of Structure of Mycobacterial Nrna Homolog Reveals Multifunctional Nuclease Activities, PDB code: 4ls9
was solved by
D.Kumar,
R.Srivastav,
A.Grover,
B.A.Manjasetty,
R.Sharma,
B.Taneja,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of Mycobacterial Nrna Homolog Reveals Multifunctional Nuclease Activities
(pdb code 4ls9). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Mycobacterial Nrna Homolog Reveals Multifunctional Nuclease Activities, PDB code: 4ls9: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 4ls9Go back to Manganese Binding Sites List in 4ls9
Manganese binding site 1 out
of 2 in the Structure of Mycobacterial Nrna Homolog Reveals Multifunctional Nuclease Activities
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 4ls9Go back to Manganese Binding Sites List in 4ls9
Manganese binding site 2 out
of 2 in the Structure of Mycobacterial Nrna Homolog Reveals Multifunctional Nuclease Activities
Mono view Stereo pair view
Reference:
R.Srivastav,
D.Kumar,
A.Grover,
A.Singh,
B.A.Manjasetty,
R.Sharma,
B.Taneja.
Unique Subunit Packing in Mycobacterial Nanornase Leads to Alternate Substrate Recognitions in Dhh Phosphodiesterases Nucleic Acids Res. V. 42 7894 2014.
Page generated: Tue Dec 15 04:24:01 2020
ISSN: ISSN 0305-1048 PubMed: 24878921 DOI: 10.1093/NAR/GKU425 |
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