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Atomistry » Manganese » PDB 1khe-1lte » 1lgb » |
Manganese in PDB 1lgb: Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose MoietyProtein crystallography data
The structure of Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety, PDB code: 1lgb
was solved by
Y.Bourne,
C.Cambillau,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1lgb:
The structure of Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety
(pdb code 1lgb). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety, PDB code: 1lgb: Manganese binding site 1 out of 1 in 1lgbGo back to Manganese Binding Sites List in 1lgb
Manganese binding site 1 out
of 1 in the Interaction of A Legume Lectin with the N2 Fragment of Human Lactotransferrin or with the Isolated Biantennary Glycopeptide: Role of the Fucose Moiety
Mono view Stereo pair view
Reference:
Y.Bourne,
J.Mazurier,
D.Legrand,
P.Rouge,
J.Montreuil,
G.Spik,
C.Cambillau.
Structures of A Legume Lectin Complexed with the Human Lactotransferrin N2 Fragment, and with An Isolated Biantennary Glycopeptide: Role of the Fucose Moiety. Structure V. 2 209 1994.
Page generated: Sat Oct 5 11:28:33 2024
ISSN: ISSN 0969-2126 PubMed: 8069634 DOI: 10.1016/S0969-2126(00)00022-8 |
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