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Atomistry » Aluminium » PDB 2xzl-3wgu » 2ybe » |
Aluminium in PDB 2ybe: The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A ResolutionEnzymatic activity of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution
All present enzymatic activity of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution:
2.7.2.3; Protein crystallography data
The structure of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution, PDB code: 2ybe
was solved by
M.W.Bowler,
L.Chaloin,
C.Lionne,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2ybe:
The structure of The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution
(pdb code 2ybe). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution, PDB code: 2ybe: Aluminium binding site 1 out of 1 in 2ybeGo back to![]() ![]()
Aluminium binding site 1 out
of 1 in the The Structure of the Fully Closed Conformation of Human Pgk in Complex with L-Adp, 3PG and the Tsa Aluminium Tetrafluoride at 2.0 A Resolution
![]() Mono view ![]() Stereo pair view
Reference:
P.Lallemand,
L.Chaloin,
B.Roy,
T.Barman,
M.W.Bowler,
C.Lionne.
Interaction of Human 3-Phosphoglycerate Kinase with Its Two Substrates: Is Substrate Antagonism A Kinetic Advantage? J.Mol.Biol. V. 409 742 2011.
Page generated: Sat Dec 12 01:32:01 2020
ISSN: ISSN 0022-2836 PubMed: 21549713 DOI: 10.1016/J.JMB.2011.04.048 |
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