1TNL: PREDICTION OF NOVEL SERINE PROTEASE INHIBITORS

Citation:
Abstract
We describe here the use of a rapid computational method to predict the relative binding strengths of a series of small-molecule ligands for the serine proteinase trypsin. Flexible molecular models of the ligands were docked to the proteinase using an all-atom potential set, without cutoff limits for the non-bonded and electrostatic energies. The binding-strength calculation is done directly in terms of a molecular mechanics potential. The binding of eighteen different compounds, including non-binding controls, has been successfully predicted. The measured Ki is correlated with the predicted energy. The correctness of the theoretical calculations is demonstrated with both kinetics measurements and X-ray structure determination of six enzyme-inhibitor complexes.
PDB ID: 1TNLDownload
MMDB ID: 51541
PDB Deposition Date: 1994/7/21
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1TNL: monomeric; determined by author
Molecular Components in 1TNL
Label Count Molecule
Protein (1 molecule)
1
Trypsin(Gene symbol: PRSS1)
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.