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Atomistry » Sodium » PDB 3ajn-3b1q » 3akg » |
Sodium in PDB 3akg: Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-ArabinofuranobioseEnzymatic activity of Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose
All present enzymatic activity of Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose:
3.2.1.55; Protein crystallography data
The structure of Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose, PDB code: 3akg
was solved by
Z.Fujimoto,
H.Ichinose,
S.Kaneko,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3akg:
The structure of Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose
(pdb code 3akg). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose, PDB code: 3akg: Sodium binding site 1 out of 1 in 3akgGo back to Sodium Binding Sites List in 3akg
Sodium binding site 1 out
of 1 in the Crystal Structure of Exo-1,5-Alpha-L-Arabinofuranosidase Complexed with Alpha-1,5-L-Arabinofuranobiose
Mono view Stereo pair view
Reference:
Z.Fujimoto,
H.Ichinose,
T.Maehara,
M.Honda,
M.Kitaoka,
S.Kaneko.
Crystal Structure of An Exo-1,5-{Alpha}-L-Arabinofuranosidase From Streptomyces Avermitilis Provides Insights Into the Mechanism of Substrate Discrimination Between Exo- and Endo-Type Enzymes in Glycoside Hydrolase Family 43. J.Biol.Chem. V. 285 34134 2010.
Page generated: Mon Oct 7 05:50:28 2024
ISSN: ISSN 0021-9258 PubMed: 20739278 DOI: 10.1074/JBC.M110.164251 |
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