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: 2024-06-05) |
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 Cited by PubMed: 1888717DOI: 10.1016/0141-8130(91)90054-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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