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Atomistry » Chlorine » PDB 4gm6-4gt9 » 4gr0 » |
Chlorine in PDB 4gr0: Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470BEnzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B
All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B:
3.4.24.65; Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B, PDB code: 4gr0
was solved by
E.A.Stura,
L.Vera,
F.Beau,
L.Devel,
E.Cassar-Lajeunesse,
V.Dive,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4gr0:
The structure of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B
(pdb code 4gr0). 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 Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B, PDB code: 4gr0: Chlorine binding site 1 out of 1 in 4gr0Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470B
![]() Mono view ![]() Stereo pair view
Reference:
B.Czarny,
E.A.Stura,
L.Devel,
L.Vera,
E.Cassar-Lajeunesse,
F.Beau,
V.Calderone,
M.Fragai,
C.Luchinat,
V.Dive.
Molecular Determinants of A Selective Matrix Metalloprotease-12 Inhibitor: Insights From Crystallography and Thermodynamic Studies. J.Med.Chem. V. 56 1149 2013.
Page generated: Fri Jul 11 15:50:45 2025
ISSN: ISSN 0022-2623 PubMed: 23343195 DOI: 10.1021/JM301574D |
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