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Atomistry » Potassium » PDB 2adp-2c13 » 2ats | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 2adp-2c13 » 2ats » |
Potassium in PDB 2ats: Dihydrodipicolinate Synthase Co-Crystallised with (S)-LysineEnzymatic activity of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine
All present enzymatic activity of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine:
4.2.1.52; Protein crystallography data
The structure of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine, PDB code: 2ats
was solved by
S.R.A.Devenish,
R.C.J.Dobson,
G.B.Jameson,
J.A.Gerrard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2ats:
The structure of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine
(pdb code 2ats). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine, PDB code: 2ats: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 2atsGo back to Potassium Binding Sites List in 2ats
Potassium binding site 1 out
of 2 in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 2atsGo back to Potassium Binding Sites List in 2ats
Potassium binding site 2 out
of 2 in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine
Mono view Stereo pair view
Reference:
S.R.A.Devenish,
R.C.J.Dobson,
G.B.Jameson,
J.A.Gerrard.
The Co-Crystallisation of (S)-Lysine-Bound Dihydrodipicolinate Synthase From E. Coli Indicates That Domain Movements Are Not Responsible For (S)-Lysine Inhibition To Be Published.
Page generated: Sun Dec 13 23:08:51 2020
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