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Chlorine in PDB 6eqw: X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-AmbaEnzymatic activity of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba
All present enzymatic activity of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba:
3.4.21.75; Protein crystallography data
The structure of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba, PDB code: 6eqw
was solved by
S.O.Dahms,
M.E.Than,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6eqw:
The structure of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba
(pdb code 6eqw). 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 X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba, PDB code: 6eqw: Chlorine binding site 1 out of 1 in 6eqwGo back to Chlorine Binding Sites List in 6eqw
Chlorine binding site 1 out
of 1 in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor 4-Aminomethyl-Phenylacetyl-Arg-Val-Arg-Amba
Mono view Stereo pair view
Reference:
S.O.Dahms,
K.Hardes,
T.Steinmetzer,
M.E.Than.
X-Ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants Beyond the S4 Pocket. Biochemistry V. 57 925 2018.
Page generated: Sat Dec 12 12:56:09 2020
ISSN: ISSN 1520-4995 PubMed: 29314830 DOI: 10.1021/ACS.BIOCHEM.7B01124 |
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