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Atomistry » Cobalt » PDB 1hv9-1nr5 » 1nr5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 1hv9-1nr5 » 1nr5 » |
Cobalt in PDB 1nr5: Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and CarbaphosphonateEnzymatic activity of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate
All present enzymatic activity of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate:
4.2.3.4; Protein crystallography data
The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate, PDB code: 1nr5
was solved by
C.E.Nichols,
J.Ren,
H.K.Lamb,
A.R.Hawkins,
D.K.Stammers,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1nr5:
The structure of Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate
(pdb code 1nr5). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate, PDB code: 1nr5: Cobalt binding site 1 out of 1 in 1nr5Go back to Cobalt Binding Sites List in 1nr5
Cobalt binding site 1 out
of 1 in the Crystal Structure of 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+, Nad and Carbaphosphonate
Mono view Stereo pair view
Reference:
C.E.Nichols,
J.Ren,
H.K.Lamb,
A.R.Hawkins,
D.K.Stammers.
Ligand-Induced Conformational Changes and A Mechanism For Domain Closure in Aspergillus Nidulans Dehydroquinate Synthase J.Mol.Biol. V. 327 129 2003.
Page generated: Tue Jul 30 14:27:15 2024
ISSN: ISSN 0022-2836 PubMed: 12614613 DOI: 10.1016/S0022-2836(03)00086-X |
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