Home

Cluster 2GMT T2 A75

The binding interfaces of the superposed protein-peptide complexes are shown in grey, the peptides in red. Images produced by YASARA. Note that only the interface of the protein-peptide complexes is shown. Gaps between residues may occur.

Properties of this cluster

2GMT
33
2 Å
75 %
Properties of this cluster. Learn more about the clustering methodology.

Protein-peptide complexes in this cluster

Showing 11-20 of 33 results
PDB ID Description
3BG4 The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor
3GCH CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN
6GCH STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS
1CA0 BOVINE CHYMOTRYPSIN COMPLEXED TO APPI
2GMT THREE-DIMENSIONAL STRUCTURE OF CHYMOTRYPSIN INACTIVATED WITH (2S) N-ACETYL-L-ALANYL-L-PHENYLALANYL-CHLOROETHYL KETONE: IMPLICATIONS FOR THE MECHANISM OF INACTIVATION OF SERINE PROTEASES BY CHLOROKETONES
2GCT STRUCTURE OF GAMMA-CHYMOTRYPSIN IN THE RANGE PH 2.0 TO PH 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW PH
1DLK CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR
1YPH High resolution structure of bovine alpha-chymotrypsin
2JET CRYSTAL STRUCTURE OF A TRYPSIN-LIKE MUTANT (S189D, A226G) CHYMOTRYPSIN.
7GCH STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS