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Atomistry » Zinc » PDB 1x81-1xm4 » 1xah » |
Zinc in PDB 1xah: Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+Enzymatic activity of Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+
All present enzymatic activity of Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+:
4.2.3.4; Protein crystallography data
The structure of Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+, PDB code: 1xah
was solved by
C.E.Nichols,
J.Ren,
K.Leslie,
B.Dhaliwal,
M.Lockyer,
I.Charles,
A.R.Hawkins,
D.K.Stammers,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+
(pdb code 1xah). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+, PDB code: 1xah: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1xahGo back to Zinc Binding Sites List in 1xah
Zinc binding site 1 out
of 2 in the Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1xahGo back to Zinc Binding Sites List in 1xah
Zinc binding site 2 out
of 2 in the Crystal Structure of Staphlyococcus Aureus 3-Dehydroquinate Synthase (Dhqs) in Complex with ZN2+ and Nad+
Mono view Stereo pair view
Reference:
C.E.Nichols,
J.Ren,
K.Leslie,
B.Dhaliwal,
M.Lockyer,
I.Charles,
A.R.Hawkins,
D.K.Stammers.
Comparison of Ligand Induced Conformational Changes and Domain Closure Mechanisms, Between Prokaryotic and Eukaryotic Dehydroquinate Synthases. J.Mol.Biol. V. 343 533 2004.
Page generated: Wed Oct 16 20:20:58 2024
ISSN: ISSN 0022-2836 PubMed: 15465043 DOI: 10.1016/J.JMB.2004.08.039 |
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