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Atomistry » Zinc » PDB 2y7e-2yql » 2yb9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2y7e-2yql » 2yb9 » |
Zinc in PDB 2yb9: Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid.Enzymatic activity of Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid.
All present enzymatic activity of Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid.:
3.4.24.11; Protein crystallography data
The structure of Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid., PDB code: 2yb9
was solved by
M.S.Glossop,
R.J.Bazin,
K.N.Dack,
S.Done,
D.N.A.Fox,
G.A.Macdonald,
M.Mills,
D.R.Owen,
C.Phillips,
K.A.Reeves,
T.J.Ringer,
R.S.Strang,
C.A.L.Watson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid.
(pdb code 2yb9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid., PDB code: 2yb9: Zinc binding site 1 out of 1 in 2yb9Go back to Zinc Binding Sites List in 2yb9
Zinc binding site 1 out
of 1 in the Crystal Structure of Human Neutral Endopeptidase Complexed with A Heteroarylalanine Diacid.
Mono view Stereo pair view
Reference:
M.S.Glossop,
R.J.Bazin,
K.N.Dack,
D.N.A.Fox,
G.A.Macdonald,
M.Mills,
D.R.Owen,
C.Phillips,
K.A.Reeves,
T.J.Ringer,
R.S.Strang,
C.A.L.Watson.
Synthesis and Evaluation of Heteroarylalanine Diacids As Potent and Selective Neutral Endopeptidase Inhibitors. Bioorg.Med.Chem.Lett. V. 21 3404 2011.
Page generated: Wed Dec 16 04:01:54 2020
ISSN: ISSN 0960-894X PubMed: 21515054 DOI: 10.1016/J.BMCL.2011.03.109 |
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