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Atomistry » Zinc » PDB 2a25-2aer » 2a8h » |
Zinc in PDB 2a8h: Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate InhibitorEnzymatic activity of Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor
All present enzymatic activity of Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor:
3.4.24.86; Protein crystallography data
The structure of Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor, PDB code: 2a8h
was solved by
J.I.Levin,
J.M.Chen,
L.M.Laakso,
M.Du,
J.Schmid,
W.Xu,
T.Cummons,
J.Xu,
G.Jin,
D.Barone,
J.S.Skotnicki,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor
(pdb code 2a8h). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor, PDB code: 2a8h: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2a8hGo back to Zinc Binding Sites List in 2a8h
Zinc binding site 1 out
of 2 in the Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2a8hGo back to Zinc Binding Sites List in 2a8h
Zinc binding site 2 out
of 2 in the Crystal Structure of Catalytic Domain of Tace with Thiomorpholine Sulfonamide Hydroxamate Inhibitor
Mono view Stereo pair view
Reference:
J.I.Levin,
J.M.Chen,
L.M.Laakso,
M.Du,
J.Schmid,
W.Xu,
T.Cummons,
J.Xu,
G.Jin,
D.Barone,
J.S.Skotnicki.
Acetylenic Tace Inhibitors. Part 3: Thiomorpholine Sulfonamide Hydroxamates. Bioorg.Med.Chem.Lett. V. 16 1605 2006.
Page generated: Wed Dec 16 03:16:59 2020
ISSN: ISSN 0960-894X PubMed: 16426848 DOI: 10.1016/J.BMCL.2005.12.020 |
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