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Atomistry » Calcium » PDB 1byn-1c5v » 1c2h | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1byn-1c5v » 1c2h » |
Calcium in PDB 1c2h: 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: 1c2h
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 1c2h:
The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases
(pdb code 1c2h). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2h: Calcium binding site 1 out of 1 in 1c2hGo back to![]() ![]()
Calcium 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 Jul 7 13:52:08 2025
ISSN: ISSN 0028-0836 PubMed: 9468142 DOI: 10.1038/35422 |
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