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Atomistry » Chlorine » PDB 3akg-3avh » 3ap9 » |
Chlorine in PDB 3ap9: Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose IIIProtein crystallography data
The structure of Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose III, PDB code: 3ap9
was solved by
T.Matsuzaka,
H.Ideo,
K.Yamashita,
T.Nonaka,
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 Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose III
(pdb code 3ap9). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose III, PDB code: 3ap9: Jump to Chlorine binding site number: 1; 2; 3; Chlorine binding site 1 out of 3 in 3ap9Go back to![]() ![]()
Chlorine binding site 1 out
of 3 in the Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose III
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 3 in 3ap9Go back to![]() ![]()
Chlorine binding site 2 out
of 3 in the Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose III
![]() Mono view ![]() Stereo pair view
Chlorine binding site 3 out of 3 in 3ap9Go back to![]() ![]()
Chlorine binding site 3 out
of 3 in the Crystal Structure of the Galectin-8 N-Terminal Carbohydrate Recognition Domain in Complex with Lacto-N-Fucopentaose III
![]() Mono view ![]() Stereo pair view
Reference:
H.Ideo,
T.Matsuzaka,
T.Nonaka,
A.Seko,
K.Yamashita.
Galectin-8-N-Domain Recognition Mechanism For Sialylated and Sulfated Glycans J.Biol.Chem. V. 286 11346 2011.
Page generated: Fri Jul 11 03:09:32 2025
ISSN: ISSN 0021-9258 PubMed: 21288902 DOI: 10.1074/JBC.M110.195925 |
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