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Atomistry » Zinc » PDB 4qia-4qqu » 4qpe | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4qia-4qqu » 4qpe » |
Zinc in PDB 4qpe: Crystal Structure of Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic AcidEnzymatic activity of Crystal Structure of Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic Acid
All present enzymatic activity of Crystal Structure of Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic Acid:
3.4.11.2; Protein crystallography data
The structure of Crystal Structure of Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic Acid, PDB code: 4qpe
was solved by
B.Nocek,
R.Mulligan,
L.Berlicki,
S.Vassilious,
A.Mucha,
A.Joachimiak,
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 Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic Acid
(pdb code 4qpe). 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 Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic Acid, PDB code: 4qpe: Zinc binding site 1 out of 1 in 4qpeGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Aminopeptidase N in Complex with N-Cyclohexyl-1, 2-Diaminoethylphosphonic Acid
![]() Mono view ![]() Stereo pair view
Reference:
S.Vassiliou,
E.Weglarz-Tomczak,
L.Berlicki,
M.Paweczak,
B.Nocek,
R.Mulligan,
A.Joachimiak,
A.Mucha.
Structure-Guided, Single-Point Modifications in the Phosphinic Dipeptide Structure Yield Highly Potent and Selective Inhibitors of Neutral Aminopeptidases. J.Med.Chem. V. 57 8140 2014.
Page generated: Sun Oct 27 06:42:35 2024
ISSN: ISSN 0022-2623 PubMed: 25192493 DOI: 10.1021/JM501071F |
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