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Atomistry » Chlorine » PDB 1byz-1c6n » 1c2l | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1byz-1c6n » 1c2l » |
Chlorine in PDB 1c2l: 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: 1c2l
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 1c2l:
The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases
(pdb code 1c2l). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2l: Chlorine binding site 1 out of 1 in 1c2lGo back to Chlorine Binding Sites List in 1c2l
Chlorine 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: Sat Dec 12 08:32:18 2020
ISSN: ISSN 0028-0836 PubMed: 9468142 DOI: 10.1038/35422 |
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