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Atomistry » Fluorine » PDB 1udb-1w5y » 1usn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Fluorine » PDB 1udb-1w5y » 1usn » |
Fluorine in PDB 1usn: Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372Enzymatic activity of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372:
3.4.24.17; Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372, PDB code: 1usn
was solved by
B.C.Finzel,
G.L.Bryant Junior,
E.T.Baldwin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1usn:
The structure of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
(pdb code 1usn). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 5 binding sites of Fluorine where determined in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372, PDB code: 1usn: Jump to Fluorine binding site number: 1; 2; 3; 4; 5; Fluorine binding site 1 out of 5 in 1usnGo back to Fluorine Binding Sites List in 1usn
Fluorine binding site 1 out
of 5 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
Mono view Stereo pair view
Fluorine binding site 2 out of 5 in 1usnGo back to Fluorine Binding Sites List in 1usn
Fluorine binding site 2 out
of 5 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
Mono view Stereo pair view
Fluorine binding site 3 out of 5 in 1usnGo back to Fluorine Binding Sites List in 1usn
Fluorine binding site 3 out
of 5 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
Mono view Stereo pair view
Fluorine binding site 4 out of 5 in 1usnGo back to Fluorine Binding Sites List in 1usn
Fluorine binding site 4 out
of 5 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
Mono view Stereo pair view
Fluorine binding site 5 out of 5 in 1usnGo back to Fluorine Binding Sites List in 1usn
Fluorine binding site 5 out
of 5 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with Thiadiazole Inhibitor Pnu-142372
Mono view Stereo pair view
Reference:
B.C.Finzel,
E.T.Baldwin,
G.L.Bryant Jr.,
G.F.Hess,
J.W.Wilks,
C.M.Trepod,
J.E.Mott,
V.P.Marshall,
G.L.Petzold,
R.A.Poorman,
T.J.O'sullivan,
H.J.Schostarez,
M.A.Mitchell.
Structural Characterizations of Nonpeptidic Thiadiazole Inhibitors of Matrix Metalloproteinases Reveal the Basis For Stromelysin Selectivity. Protein Sci. V. 7 2118 1998.
Page generated: Wed Jul 31 13:03:05 2024
ISSN: ISSN 0961-8368 PubMed: 9792098 |
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