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Fluorine in PDB 7wxx: Crystal Structure of Human Mmp-7 in Complex with InhibitorEnzymatic activity of Crystal Structure of Human Mmp-7 in Complex with Inhibitor
All present enzymatic activity of Crystal Structure of Human Mmp-7 in Complex with Inhibitor:
3.4.24.23; Protein crystallography data
The structure of Crystal Structure of Human Mmp-7 in Complex with Inhibitor, PDB code: 7wxx
was solved by
M.Kamitani,
Y.Oka,
H.Tabuse,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7wxx:
The structure of Crystal Structure of Human Mmp-7 in Complex with Inhibitor also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor
(pdb code 7wxx). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor, PDB code: 7wxx: Jump to Fluorine binding site number: 1; 2; 3; Fluorine binding site 1 out of 3 in 7wxxGo back to Fluorine Binding Sites List in 7wxx
Fluorine binding site 1 out
of 3 in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor
Mono view Stereo pair view
Fluorine binding site 2 out of 3 in 7wxxGo back to Fluorine Binding Sites List in 7wxx
Fluorine binding site 2 out
of 3 in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor
Mono view Stereo pair view
Fluorine binding site 3 out of 3 in 7wxxGo back to Fluorine Binding Sites List in 7wxx
Fluorine binding site 3 out
of 3 in the Crystal Structure of Human Mmp-7 in Complex with Inhibitor
Mono view Stereo pair view
Reference:
H.Tabuse,
K.Abe-Sato,
H.Kanazawa,
M.Yashiro,
Y.Tamura,
M.Kamitani,
K.Hitaka,
E.Gunji,
A.Mitani,
N.Kojima,
Y.Oka.
Discovery of Highly Potent and Selective Matrix Metalloproteinase-7 Inhibitors By Hybridizing the S1' Subsite Binder with Short Peptides. J.Med.Chem. V. 65 13253 2022.
Page generated: Wed Apr 5 01:47:31 2023
ISSN: ISSN 0022-2623 PubMed: 36137271 DOI: 10.1021/ACS.JMEDCHEM.2C01088 |
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