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Atomistry » Chlorine » PDB 5d0z-5da3 » 5d3c » |
Chlorine in PDB 5d3c: Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470Enzymatic activity of Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470
All present enzymatic activity of Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470:
3.4.24.65; Protein crystallography data
The structure of Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470, PDB code: 5d3c
was solved by
C.Rouanet-Mehouas,
L.Devel,
V.Dive,
E.A.Stura,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5d3c:
The structure of Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470
(pdb code 5d3c). 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 A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470, PDB code: 5d3c: Chlorine binding site 1 out of 1 in 5d3cGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of A Double Mutant Catalytic Domain of Human MMP12 in Complex with An Hydroxamate Analogue of RXP470
![]() Mono view ![]() Stereo pair view
Reference:
C.Rouanet-Mehouas,
B.Czarny,
F.Beau,
E.Cassar-Lajeunesse,
E.A.Stura,
V.Dive,
L.Devel.
Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played By the Zinc-Binding Group on Potency and Selectivity. J. Med. Chem. V. 60 403 2017.
Page generated: Sat Jul 12 01:06:02 2025
ISSN: ISSN 1520-4804 PubMed: 27996256 DOI: 10.1021/ACS.JMEDCHEM.6B01420 |
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