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Atomistry » Magnesium » PDB 4u9i-4um5 » 4uhd | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 4u9i-4um5 » 4uhd » |
Magnesium in PDB 4uhd: Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)Enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)
All present enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound):
3.1.1.1; Protein crystallography data
The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound), PDB code: 4uhd
was solved by
C.Sayer,
M.N.Isupov,
E.Bonch-Osmolovskaya,
J.A.Littlechild,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4uhd:
The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)
(pdb code 4uhd). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound), PDB code: 4uhd: Magnesium binding site 1 out of 1 in 4uhdGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)
![]() Mono view ![]() Stereo pair view
Reference:
C.Sayer,
M.N.Isupov,
E.Bonch-Osmolovskaya,
J.A.Littlechild.
Structural Studies of A Thermophilic Esterase From A New Planctomycetes Species, Thermogutta Terrifontis. Febs J. V. 282 2846 2015.
Page generated: Tue Aug 20 04:43:14 2024
ISSN: ISSN 1742-464X PubMed: 26011036 DOI: 10.1111/FEBS.13326 |
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