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Atomistry » Calcium » PDB 1gxr-1h71 » 1gz9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1gxr-1h71 » 1gz9 » |
Calcium in PDB 1gz9: High-Resolution Crystal Structure of Erythrina Cristagalli Lectin in Complex with 2'-Alpha-L-FucosyllactoseProtein crystallography data
The structure of High-Resolution Crystal Structure of Erythrina Cristagalli Lectin in Complex with 2'-Alpha-L-Fucosyllactose, PDB code: 1gz9
was solved by
C.Svensson,
S.Teneberg,
C.L.Nilsson,
A.Kjellberg,
F.P.Schwarz,
N.Sharon,
U.Krengel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1gz9:
The structure of High-Resolution Crystal Structure of Erythrina Cristagalli Lectin in Complex with 2'-Alpha-L-Fucosyllactose also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the High-Resolution Crystal Structure of Erythrina Cristagalli Lectin in Complex with 2'-Alpha-L-Fucosyllactose
(pdb code 1gz9). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the High-Resolution Crystal Structure of Erythrina Cristagalli Lectin in Complex with 2'-Alpha-L-Fucosyllactose, PDB code: 1gz9: Calcium binding site 1 out of 1 in 1gz9Go back to![]() ![]()
Calcium binding site 1 out
of 1 in the High-Resolution Crystal Structure of Erythrina Cristagalli Lectin in Complex with 2'-Alpha-L-Fucosyllactose
![]() Mono view ![]() Stereo pair view
Reference:
C.Svensson,
S.Teneberg,
C.L.Nilsson,
A.Kjellberg,
F.P.Schwarz,
N.Sharon,
U.Krengel.
High-Resolution Crystal Structures of Erythrina Cristagalli Lectin in Complex with Lactose and 2'-Alpha-L-Fucosyllactose and Correlation with Thermodynamic Binding Data J.Mol.Biol. V. 321 69 2002.
Page generated: Mon Jul 7 15:26:13 2025
ISSN: ISSN 0022-2836 PubMed: 12139934 DOI: 10.1016/S0022-2836(02)00554-5 |
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