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

Summary for 2GCT

• Entry DOI: 10.2210/pdb2gct/pdb
• Related: 1GCT 3GCT
• Descriptor: GAMMA-CHYMOTRYPSIN A, TETRAPEPTIDE ADDUCT, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, serine proteinase, hydrolase-peptide complex, hydrolase/peptide
• Biological source: Bos taurus; More
• Cellular location: Secreted, extracellular space: P00766 P00766 P00766
• Total number of polymer chains: 4
• Total formula weight: 25946.23

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 (1.8 Å)