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Atomistry » Calcium » PDB 6i1t-6im1 » 6ifd | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 6i1t-6im1 » 6ifd » |
Calcium in PDB 6ifd: Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.Enzymatic activity of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.
All present enzymatic activity of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.:
2.7.7.43; Protein crystallography data
The structure of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+., PDB code: 6ifd
was solved by
S.Bose,
R.Subramanian,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6ifd:
The structure of Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+. also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.
(pdb code 6ifd). 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 Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+., PDB code: 6ifd: Calcium binding site 1 out of 1 in 6ifdGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae in Complex with Cdp and MG2+.
![]() Mono view ![]() Stereo pair view
Reference:
S.Bose,
D.Purkait,
D.Joseph,
V.Nayak,
R.Subramanian.
Structural and Functional Characterization of Cmp-N-Acetylneuraminate Synthetase From Vibrio Cholerae. Acta Crystallogr D Struct V. 75 564 2019BIOL.
Page generated: Wed Jul 9 14:50:54 2025
ISSN: ISSN 2059-7983 PubMed: 31205019 DOI: 10.1107/S2059798319006831 |
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