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Atomistry » Potassium » PDB 1yjn-2aaq » 1yxc | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 1yjn-2aaq » 1yxc » |
Potassium in PDB 1yxc: Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 AEnzymatic activity of Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A
All present enzymatic activity of Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A:
4.2.1.52; Protein crystallography data
The structure of Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A, PDB code: 1yxc
was solved by
R.C.J.Dobson,
M.D.W.Griffin,
G.B.Jameson,
J.A.Gerrard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1yxc:
The structure of Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A
(pdb code 1yxc). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A, PDB code: 1yxc: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 1yxcGo back to Potassium Binding Sites List in 1yxc
Potassium binding site 1 out
of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 1yxcGo back to Potassium Binding Sites List in 1yxc
Potassium binding site 2 out
of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase to 1.9 A
Mono view Stereo pair view
Reference:
R.C.Dobson,
M.D.Griffin,
G.B.Jameson,
J.A.Gerrard.
The Crystal Structures of Native and (S)-Lysine-Bound Dihydrodipicolinate Synthase From Escherichia Coli with Improved Resolution Show New Features of Biological Significance. Acta Crystallogr.,Sect.D V. 61 1116 2005.
Page generated: Mon Aug 12 05:52:52 2024
ISSN: ISSN 0907-4449 PubMed: 16041077 DOI: 10.1107/S0907444905016318 |
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