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Atomistry » Chlorine » PDB 5anv-5b1f » 5aoa | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5anv-5b1f » 5aoa » |
Chlorine in PDB 5aoa: The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate BoundEnzymatic activity of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate Bound
All present enzymatic activity of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate Bound:
3.1.1.1; Protein crystallography data
The structure of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate Bound, PDB code: 5aoa
was solved by
C.Sayer,
Z.Szabo,
M.N.Isupov,
C.Ingham,
J.A.Littlechild,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate Bound
(pdb code 5aoa). 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 The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate Bound, PDB code: 5aoa: Chlorine binding site 1 out of 1 in 5aoaGo back to Chlorine Binding Sites List in 5aoa
Chlorine binding site 1 out
of 1 in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Propionate Bound
Mono view Stereo pair view
Reference:
C.Sayer,
Z.Szabo,
M.N.Isupov,
C.Ingham,
J.A.Littlechild.
The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis Reveals An Open Active Site Due to A Minimal 'Cap' Domain. Front.Microbiol. V. 6 1294 2015.
Page generated: Sat Dec 12 11:31:11 2020
ISSN: ESSN 1664-302X PubMed: 26635762 DOI: 10.3389/FMICB.2015.01294 |
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