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Atomistry » Iodine » PDB 2nqx-2qpy » 2ogs » |
Iodine in PDB 2ogs: Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2Enzymatic activity of Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2
All present enzymatic activity of Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2:
3.1.1.1; Protein crystallography data
The structure of Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2, PDB code: 2ogs
was solved by
P.Liu,
H.E.Ewis,
P.C.Tai,
C.D.Lu,
I.T.Weber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iodine Binding Sites:
The binding sites of Iodine atom in the Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2
(pdb code 2ogs). This binding sites where shown within
5.0 Angstroms radius around Iodine atom.
In total 3 binding sites of Iodine where determined in the Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2, PDB code: 2ogs: Jump to Iodine binding site number: 1; 2; 3; Iodine binding site 1 out of 3 in 2ogsGo back to Iodine Binding Sites List in 2ogs
Iodine binding site 1 out
of 3 in the Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2
Mono view Stereo pair view
Iodine binding site 2 out of 3 in 2ogsGo back to Iodine Binding Sites List in 2ogs
Iodine binding site 2 out
of 3 in the Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2
Mono view Stereo pair view
Iodine binding site 3 out of 3 in 2ogsGo back to Iodine Binding Sites List in 2ogs
Iodine binding site 3 out
of 3 in the Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 at pH 6.2
Mono view Stereo pair view
Reference:
P.Liu,
H.E.Ewis,
P.C.Tai,
C.D.Lu,
I.T.Weber.
Crystal Structure of the Geobacillus Stearothermophilus Carboxylesterase EST55 and Its Activation of Prodrug Cpt-11. J.Mol.Biol. V. 367 212 2007.
Page generated: Sun Dec 13 19:24:41 2020
ISSN: ISSN 0022-2836 PubMed: 17239398 DOI: 10.1016/J.JMB.2006.12.067 |
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