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Atomistry » Bromine » PDB 4g6w-4i29 » 4gr8 » |
Bromine in PDB 4gr8: Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470CEnzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470C
All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470C:
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 RXP470C, PDB code: 4gr8
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 4gr8:
The structure of Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470C also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470C
(pdb code 4gr8). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470C, PDB code: 4gr8: Bromine binding site 1 out of 1 in 4gr8Go back to Bromine Binding Sites List in 4gr8
Bromine binding site 1 out
of 1 in the Crystal Structure of the Catalytic Domain of Human MMP12 in Complex with Selective Phosphinic Inhibitor RXP470C
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: Sat Dec 12 02:19:49 2020
ISSN: ISSN 0022-2623 PubMed: 23343195 DOI: 10.1021/JM301574D |
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