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Atomistry » Manganese » PDB 2feu-2hr6 » 2fyb » |
Manganese in PDB 2fyb: Crystal Structure of the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open ConformationEnzymatic activity of Crystal Structure of the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open Conformation
All present enzymatic activity of Crystal Structure of the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open Conformation:
2.4.1.90; Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open Conformation, PDB code: 2fyb
was solved by
B.Ramakrishnan,
V.Ramasamy,
P.K.Qasba,
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 the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open Conformation
(pdb code 2fyb). 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 the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open Conformation, PDB code: 2fyb: Manganese binding site 1 out of 1 in 2fybGo back to Manganese Binding Sites List in 2fyb
Manganese binding site 1 out
of 1 in the Crystal Structure of the Catalytic Domain of the Human BETA1,4-Galactosyltransferase Mutant M339H in Complex with Mn and Udp-Galactose in Open Conformation
Mono view Stereo pair view
Reference:
B.Ramakrishnan,
V.Ramasamy,
P.K.Qasba.
Structural Snapshots of Beta-1,4-Galactosyltransferase-I Along the Kinetic Pathway. J.Mol.Biol. V. 357 1619 2006.
Page generated: Tue Dec 15 04:01:52 2020
ISSN: ISSN 0022-2836 PubMed: 16497331 DOI: 10.1016/J.JMB.2006.01.088 |
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