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Atomistry » Calcium » PDB 6bia-6bxu » 6bmt » |
Calcium 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:
Calcium Binding Sites:
The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of A Recombinant Form of Human Myeloperoxidase Bound to An Inhibitor From Staphylococcus Delphini, PDB code: 6bmt: Calcium binding site 1 out of 1 in 6bmtGo back to Calcium Binding Sites List in 6bmt
Calcium 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: Mon Jul 15 17:01:31 2024
ISSN: ESSN 1096-0384 PubMed: 29524428 DOI: 10.1016/J.ABB.2018.03.007 |
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