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Atomistry » Zinc » PDB 6r55-6rda » 6rd0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 6r55-6rda » 6rd0 » |
Zinc in PDB 6rd0: Human MMP12 Catalytic Domain in Complex with AP280Enzymatic activity of Human MMP12 Catalytic Domain in Complex with AP280
All present enzymatic activity of Human MMP12 Catalytic Domain in Complex with AP280:
3.4.24.65; Protein crystallography data
The structure of Human MMP12 Catalytic Domain in Complex with AP280, PDB code: 6rd0
was solved by
V.Calderone,
M.Fragai,
C.Luchinat,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6rd0:
The structure of Human MMP12 Catalytic Domain in Complex with AP280 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Human MMP12 Catalytic Domain in Complex with AP280
(pdb code 6rd0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human MMP12 Catalytic Domain in Complex with AP280, PDB code: 6rd0: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 6rd0Go back to![]() ![]()
Zinc binding site 1 out
of 2 in the Human MMP12 Catalytic Domain in Complex with AP280
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 6rd0Go back to![]() ![]()
Zinc binding site 2 out
of 2 in the Human MMP12 Catalytic Domain in Complex with AP280
![]() Mono view ![]() Stereo pair view
Reference:
S.Tsoukalidou,
M.Kakou,
I.Mavridis,
D.Koumantou,
V.Calderone,
M.Fragai,
E.Stratikos,
A.Papakyriakou,
D.Vourloumis.
Exploration of Zinc-Binding Groups For the Design of Inhibitors For the Oxytocinase Subfamily of M1 Aminopeptidases. Bioorg.Med.Chem. V. 27 15177 2019.
Page generated: Tue Oct 29 06:11:52 2024
ISSN: ESSN 1464-3391 PubMed: 31711716 DOI: 10.1016/J.BMC.2019.115177 |
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