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Atomistry » Potassium » PDB 1m5h-1o07 » 1mc5 » |
Potassium in PDB 1mc5: Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and NadhEnzymatic activity of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh
All present enzymatic activity of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh:
1.1.1.1; 1.2.1.1; Protein crystallography data
The structure of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh, PDB code: 1mc5
was solved by
P.C.Sanghani,
W.F.Bosron,
T.D.Hurley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1mc5:
The structure of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh
(pdb code 1mc5). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh, PDB code: 1mc5: Potassium binding site 1 out of 1 in 1mc5Go back to![]() ![]()
Potassium binding site 1 out
of 1 in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh
![]() Mono view ![]() Stereo pair view
Reference:
P.C.Sanghani,
W.F.Bosron,
T.D.Hurley.
Human Glutathione-Dependent Formaldehyde Dehydrogenase. Structural Changes Associated with Ternary Complex Formation Biochemistry V. 41 15189 2002.
Page generated: Mon Aug 12 04:57:11 2024
ISSN: ISSN 0006-2960 PubMed: 12484756 DOI: 10.1021/BI026705Q |
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