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Atomistry » Chlorine » PDB 4ug5-4ui1 » 4uhh | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4ug5-4ui1 » 4uhh » |
Chlorine in PDB 4uhh: Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)Enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)
All present enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex):
3.1.1.1; Protein crystallography data
The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex), PDB code: 4uhh
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 4uhh:
The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex) also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)
(pdb code 4uhh). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex), PDB code: 4uhh: Chlorine binding site 1 out of 1 in 4uhhGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)
![]() 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: Fri Jul 26 02:18:57 2024
ISSN: ISSN 1742-464X PubMed: 26011036 DOI: 10.1111/FEBS.13326 |
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