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Atomistry » Manganese » PDB 2hvh-2jcj » 2j0b | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 2hvh-2jcj » 2j0b » |
Manganese in PDB 2j0b: Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and ManganeseEnzymatic activity of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese
All present enzymatic activity of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese:
2.4.1.222; Protein crystallography data
The structure of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese, PDB code: 2j0b
was solved by
M.Jinek,
Y.-W.Chen,
H.Clausen,
S.M.Cohen,
E.Conti,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2j0b:
The structure of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese
(pdb code 2j0b). 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 Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese, PDB code: 2j0b: Manganese binding site 1 out of 1 in 2j0bGo back to Manganese Binding Sites List in 2j0b
Manganese binding site 1 out
of 1 in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese
Mono view Stereo pair view
Reference:
M.Jinek,
Y.-W.Chen,
H.Clausen,
S.M.Cohen,
E.Conti.
Structural Insights Into the Notch-Modifying Glycosyltransferase Fringe Nat.Struct.Mol.Biol. V. 13 945 2006.
Page generated: Tue Dec 15 04:03:00 2020
ISSN: ISSN 1545-9993 PubMed: 16964258 DOI: 10.1038/NSMB1144 |
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