3GCT

STRUCTURE OF GAMMA-*CHYMOTRYPSIN IN THE RANGE $P*H 2.0 TO $P*H 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW $P*H

Summary for 3GCT

• Entry DOI: 10.2210/pdb3gct/pdb
• Related: 2GCT 3GCT
• Descriptor: GAMMA-CHYMOTRYPSIN A, UNK PRO GLY ALA TYR PEPTIDE, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, serine proteinase, hydrolase-peptide complex, hydrolase/peptide
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted, extracellular space: P00766 P00766 P00766
• Total number of polymer chains: 4
• Total formula weight: 25850.16

Authors

Dixon, M.M.,Matthews, B.W. (deposition date: 1990-09-04, release date: 1991-10-15, Last modification date: 2013-03-13)

• Primary citation: Dixon, M.M.,Brennan, R.G.,Matthews, B.W.; 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.; Int.J.Biol.Macromol., 13:89-96, 1991; PubMed: 1888717; DOI: 10.1016/0141-8130(91)90054-X

Experimental method

X-RAY DIFFRACTION (1.6 Å)