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: 2011-07-13)
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: 7947790 DOI: 10.1021/bi00250a033 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation