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
Summary for 2GMT
Entry DOI | 10.2210/pdb2gmt/pdb |
Descriptor | GAMMA-CHYMOTRYPSIN, (2S) N-ACETYL-L-ALANYL-ALPHAL-PHENYLALANYL-CHLOROETHYLKETONE, ... (5 entities in total) |
Functional Keywords | hydrolase(serine proteinase) |
Biological source | Bos taurus (cattle) |
Cellular location | Secreted, extracellular space: P00766 P00766 P00766 |
Total number of polymer chains | 3 |
Total formula weight | 25587.37 |
Authors | Kreutter, K.,Steinmetz, A.C.U.,Liang, T.-C.,Prorok, M.,Abeles, R.,Ringe, D. (deposition date: 1994-09-07, release date: 1994-11-01, Last modification date: 2024-06-05) |
Primary citation | Kreutter, K.,Steinmetz, A.C.,Liang, T.C.,Prorok, M.,Abeles, R.H.,Ringe, D. Three-dimensional structure of chymotrypsin inactivated with (2S)-N-acetyl-L-alanyl-L-phenylalanyl alpha-chloroethane: implications for the mechanism of inactivation of serine proteases by chloroketones. Biochemistry, 33:13792-13800, 1994 Cited by PubMed: 7947790DOI: 10.1021/bi00250a033 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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