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Atomistry » Chlorine » PDB 6bmr-6bry » 6bmt » |
Chlorine in PDB 6bmt: Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus DelphiniEnzymatic activity of Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini
All present enzymatic activity of Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini:
1.11.2.2; Protein crystallography data
The structure of Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini, PDB code: 6bmt
was solved by
N.T.Ploscariu,
B.V.Geisbrecht,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6bmt:
The structure of Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini
(pdb code 6bmt). 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 Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini, PDB code: 6bmt: Chlorine binding site 1 out of 1 in 6bmtGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini
![]() Mono view ![]() Stereo pair view
Reference:
N.T.Ploscariu,
N.W.M.De Jong,
K.P.M.Van Kessel,
J.A.G.Van Strijp,
B.V.Geisbrecht.
Identification and Structural Characterization of A Novel Myeloperoxidase Inhibitor From Staphylococcus Delphini. Arch. Biochem. Biophys. V. 645 1 2018.
Page generated: Sat Jul 12 11:58:07 2025
ISSN: ESSN 1096-0384 PubMed: 29524428 DOI: 10.1016/J.ABB.2018.03.007 |
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