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Atomistry » Manganese » PDB 4lta-4mu3 » 4mda | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 4lta-4mu3 » 4mda » |
Manganese in PDB 4mda: Structure of MOS1 Transposase Catalytic Domain and Raltegravir with MnProtein crystallography data
The structure of Structure of MOS1 Transposase Catalytic Domain and Raltegravir with Mn, PDB code: 4mda
was solved by
J.M.Richardson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4mda:
The structure of Structure of MOS1 Transposase Catalytic Domain and Raltegravir with Mn also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of MOS1 Transposase Catalytic Domain and Raltegravir with Mn
(pdb code 4mda). 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 MOS1 Transposase Catalytic Domain and Raltegravir with Mn, PDB code: 4mda: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 4mdaGo back to Manganese Binding Sites List in 4mda
Manganese binding site 1 out
of 2 in the Structure of MOS1 Transposase Catalytic Domain and Raltegravir with Mn
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 4mdaGo back to Manganese Binding Sites List in 4mda
Manganese binding site 2 out
of 2 in the Structure of MOS1 Transposase Catalytic Domain and Raltegravir with Mn
Mono view Stereo pair view
Reference:
U.M.Wolkowicz,
E.R.Morris,
M.Robson,
M.Trubitsyna,
J.M.Richardson.
Structural Basis of MOS1 Transposase Inhibition By the Anti-Retroviral Drug Raltegravir. Acs Chem.Biol. V. 9 743 2014.
Page generated: Tue Dec 15 04:24:25 2020
ISSN: ISSN 1554-8929 PubMed: 24397848 DOI: 10.1021/CB400791U |
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