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Atomistry » Manganese » PDB 2hvh-2jcj » 2jcj | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 2hvh-2jcj » 2jcj » |
Manganese in PDB 2jcj: Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and TrisEnzymatic activity of Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and Tris
All present enzymatic activity of Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and Tris:
2.4.1.151; Protein crystallography data
The structure of Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and Tris, PDB code: 2jcj
was solved by
H.Jamaluddin,
P.Tumbale,
S.G.Withers,
K.R.Acharya,
K.Brew,
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 Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and Tris
(pdb code 2jcj). 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 Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and Tris, PDB code: 2jcj: Manganese binding site 1 out of 1 in 2jcjGo back to![]() ![]()
Manganese binding site 1 out
of 1 in the Crystal Structure of Alpha-1,3 Galactosyltransferase (C-Terminus Truncated Mutant-C3) in Complex with Udp and Tris
![]() Mono view ![]() Stereo pair view
Reference:
H.Jamaluddin,
P.Tumbale,
S.G.Withers,
K.R.Acharya,
K.Brew.
Conformational Changes Induced By Binding Udp-2F-Galactose to Alpha-1,3 Galactosyltransferase-Implications For Catalysis. J.Mol.Biol. V. 369 1270 2007.
Page generated: Sat Oct 5 14:32:23 2024
ISSN: ISSN 0022-2836 PubMed: 17493636 DOI: 10.1016/J.JMB.2007.04.012 |
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