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Atomistry » Magnesium » PDB 1bho-1c5p » 1c2e | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1bho-1c5p » 1c2e » |
Magnesium in PDB 1c2e: Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine ProteasesEnzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases
All present enzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases:
3.4.21.4; Protein crystallography data
The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2e
was solved by
B.A.Katz,
C.Luong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1c2e:
The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases
(pdb code 1c2e). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2e: Magnesium binding site 1 out of 1 in 1c2eGo back to Magnesium Binding Sites List in 1c2e
Magnesium binding site 1 out
of 1 in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases
Mono view Stereo pair view
Reference:
B.A.Katz,
J.M.Clark,
J.S.Finer-Moore,
T.E.Jenkins,
C.R.Johnson,
M.J.Ross,
C.Luong,
W.R.Moore,
R.M.Stroud.
Design of Potent Selective Zinc-Mediated Serine Protease Inhibitors. Nature V. 391 608 1998.
Page generated: Mon Dec 14 05:48:10 2020
ISSN: ISSN 0028-0836 PubMed: 9468142 DOI: 10.1038/35422 |
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