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Atomistry » Potassium » PDB 1yjn-2aaq » 2a6v | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 1yjn-2aaq » 2a6v » |
Potassium in PDB 2a6v: Crystal Structure of EMP46P Carbohydrate Recognition Domain (Crd), Potassium-Bound FormProtein crystallography data
The structure of Crystal Structure of EMP46P Carbohydrate Recognition Domain (Crd), Potassium-Bound Form, PDB code: 2a6v
was solved by
T.Satoh,
K.Sato,
A.Kanoh,
K.Yamashita,
R.Kato,
A.Nakano,
S.Wakatsuki,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of EMP46P Carbohydrate Recognition Domain (Crd), Potassium-Bound Form
(pdb code 2a6v). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of EMP46P Carbohydrate Recognition Domain (Crd), Potassium-Bound Form, PDB code: 2a6v: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 2a6vGo back to Potassium Binding Sites List in 2a6v
Potassium binding site 1 out
of 2 in the Crystal Structure of EMP46P Carbohydrate Recognition Domain (Crd), Potassium-Bound Form
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 2a6vGo back to Potassium Binding Sites List in 2a6v
Potassium binding site 2 out
of 2 in the Crystal Structure of EMP46P Carbohydrate Recognition Domain (Crd), Potassium-Bound Form
Mono view Stereo pair view
Reference:
T.Satoh,
K.Sato,
A.Kanoh,
K.Yamashita,
Y.Yamada,
N.Igarashi,
R.Kato,
A.Nakano,
S.Wakatsuki.
Structures of the Carbohydrate Recognition Domain of CA2+-Independent Cargo Receptors EMP46P and EMP47P. J.Biol.Chem. V. 281 10410 2006.
Page generated: Mon Aug 12 06:00:18 2024
ISSN: ISSN 0021-9258 PubMed: 16439369 DOI: 10.1074/JBC.M512258200 |
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