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Atomistry » Calcium » PDB 4r9j-4rvy » 4r9v | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 4r9j-4rvy » 4r9v » |
Calcium in PDB 4r9v: Crystal Structure of Sialyltransferase From Photobacterium Damselae, Residues 113-497 Corresponding to the Gt-B DomainProtein crystallography data
The structure of Crystal Structure of Sialyltransferase From Photobacterium Damselae, Residues 113-497 Corresponding to the Gt-B Domain, PDB code: 4r9v
was solved by
Y.Li,
N.Huynh,
X.Chen,
A.J.Fisher,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Sialyltransferase From Photobacterium Damselae, Residues 113-497 Corresponding to the Gt-B Domain
(pdb code 4r9v). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Sialyltransferase From Photobacterium Damselae, Residues 113-497 Corresponding to the Gt-B Domain, PDB code: 4r9v: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 4r9vGo back to![]() ![]()
Calcium binding site 1 out
of 2 in the Crystal Structure of Sialyltransferase From Photobacterium Damselae, Residues 113-497 Corresponding to the Gt-B Domain
![]() Mono view ![]() Stereo pair view
Calcium binding site 2 out of 2 in 4r9vGo back to![]() ![]()
Calcium binding site 2 out
of 2 in the Crystal Structure of Sialyltransferase From Photobacterium Damselae, Residues 113-497 Corresponding to the Gt-B Domain
![]() Mono view ![]() Stereo pair view
Reference:
N.Huynh,
Y.Li,
H.Yu,
S.Huang,
K.Lau,
X.Chen,
A.J.Fisher.
Crystal Structures of Sialyltransferase From Photobacterium Damselae Febs Lett. 2014.
Page generated: Sun Jul 14 12:40:15 2024
ISSN: ISSN 0014-5793 DOI: 10.1016/J.FEBSLET.2014.11.003 |
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