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Atomistry » Potassium » PDB 1a3w-1d7u » 1arz » |
Potassium in PDB 1arz: Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine DicarboxylateEnzymatic activity of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate
All present enzymatic activity of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate:
1.3.1.26; Protein crystallography data
The structure of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate, PDB code: 1arz
was solved by
G.Scapin,
S.G.Reddy,
R.Zheng,
J.S.Blanchard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate
(pdb code 1arz). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate, PDB code: 1arz: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 1arzGo back to Potassium Binding Sites List in 1arz
Potassium binding site 1 out
of 2 in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 1arzGo back to Potassium Binding Sites List in 1arz
Potassium binding site 2 out
of 2 in the Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and 2,6 Pyridine Dicarboxylate
Mono view Stereo pair view
Reference:
G.Scapin,
S.G.Reddy,
R.Zheng,
J.S.Blanchard.
Three-Dimensional Structure of Escherichia Coli Dihydrodipicolinate Reductase in Complex with Nadh and the Inhibitor 2,6-Pyridinedicarboxylate. Biochemistry V. 36 15081 1997.
Page generated: Mon Aug 12 04:02:29 2024
ISSN: ISSN 0006-2960 PubMed: 9398235 DOI: 10.1021/BI9719915 |
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