Structure for peptidase S01.001: chymotrypsin A (cattle-type)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

PDB	Organism	Resolution	Comment
1CBW_ABC	Bos taurus	2.60 Å	complex with basic pancreatic trypsin inhibitor
Only the peptidase molecule is shown. Catalytic residues are shown in ball-and-stick representation: His57 in purple, Asp102 in pink and Ser195 in orange.

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2GMT	Bos taurus	1.80 Å	gamma-chymotrypsin A; complex with N-ac-L-Ala-L-Phe-chloroethylketone
Catalytic residues are shown in ball-and-stick representation: His57 in purple, Asp102 in pink and Ser195 in orange. Ac-Ala-Phe-chloroethane is shown in grey in ball-and-stick representation.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Bos taurus
gamma-chymotrypsin	1.60 Å	1AB9	1AB9	1AB9	1AB9	1AB9	1AB9	Kashima et al., 1998
complex with eglin C	2.00 Å	1ACB	1ACB	1ACB	1ACB	1ACB	1ACB	Frigerio et al., 1992
complex with D-Leu-Phe-fluorobenzylamine	1.80 Å	1AFQ	1AFQ	1AFQ	1AFQ	1AFQ	1AFQ	Yennawar et al., 1994
complex with inhibitor domain of Alzheimer's amyloid protein	2.10 Å	1CA0	1CA0	1CA0	1CA0	1CA0	1CA0	Scheidig et al., 1997
complex with basic pancreatic trypsin inhibitor	2.60 Å	1CBW	1CBW	1CBW	1CBW	1CBW	1CBW	Scheidig et al., 1997
complex with human pancreatic secretory trypsin inhibitor variant 3	2.30 Å	1CGI	1CGI	1CGI	1CGI	1CGI	1CGI	Hecht et al., 1991
complex with human pancreatic secretory trypsin inhibitor variant 4	2.30 Å	1CGJ	1CGJ	1CGJ	1CGJ	1CGJ	1CGJ	Hecht et al., 1991
zymogen	2.50 Å	1CHG	1CHG	1CHG	1CHG	1CHG	1CHG
complex with turkey ovomucoid third domain	1.80 Å	1CHO	1CHO	1CHO	1CHO	1CHO	1CHO	Fujinaga et al., 1987
delta form; complex with benzyloxycarbonyl-Gly-Gly-Phe-chloromethane	2.14 Å	1DLK	1DLK	1DLK	1DLK	1DLK	1DLK	Mac et al., 2000
precursor	3.00 Å	1EX3	1EX3	1EX3	1EX3	1EX3	1EX3	Pjura et al., 2000
complex with diethyl phosphoryl	1.90 Å	1GCD	1GCD	1GCD	1GCD	1GCD	1GCD	Harel et al., 1991
gamma-chymotrypsin A	1.60 Å	1GCT	1GCT	1GCT	1GCT	1GCT	1GCT	Dixon & Matthews, 1989
complex with N-acetyl-Phe trifluoromethyl ketone	1.40 Å	1GG6	1GG6	1GG6	1GG6	1GG6	1GG6	Neidhart et al., 2001
gamma form; complex with N-acetyl-Leu-Phe-aldehyde	1.50 Å	1GGD	1GGD	1GGD	1GGD	1GGD	1GGD	Neidhart et al., 2001
in 4% isopropanol	2.20 Å	1GHA	1GHA	1GHA	1GHA	1GHA	1GHA
complex with N-acetyl-D-tryptophan	2.00 Å	1GHB	1GHB	1GHB	1GHB	1GHB	1GHB
complex with PMP-D2V inhibitor from migratory locust	3.00 Å	1GL0	1GL0	1GL0	1GL0	1GL0	1GL0	Roussel et al., 2001
complex with PMP-C inhibitor from migratory locust	2.10 Å	1GL1	1GL1	1GL1	1GL1	1GL1	1GL1	Roussel et al., 2001
gamma-chymotrypsin	2.20 Å	1GMC	1GMC	1GMC	1GMC	1GMC	1GMC	Yennawar et al., 1994
gamma-chymotrypsin	2.20 Å	1GMD	1GMD	1GMD	1GMD	1GMD	1GMD	Yennawar et al., 1994
complex with diisopropylphosphorofluoridate	2.10 Å	1GMH	1GMH	1GMH	1GMH	1GMH	1GMH	Harel et al., 1991
complex with turkey ovomucoid inhibitor third domain	2.30 Å	1HJA	1HJA	1HJA	1HJA	1HJA	1HJA
complex with 7-hydroxycoumarin	1.80 Å	1K2I	1K2I	1K2I	1K2I	1K2I	1K2I	Ghani et al., 2001
alpha-chymotrypsin; complex with basic pancreatic trypsin inhibitor	2.80 Å	1MTN	1MTN	1MTN	1MTN	1MTN	1MTN	Capasso et al., 1997
complex with ecotin	2.00 Å	1N8O	1N8O	1N8O	1N8O	1N8O	1N8O
complex with autocatalytically produced 14-residue peptide	2.20 Å	1OXG	1OXG	1OXG	1OXG	1OXG	1OXG	Singh et al., 2005
complex with aprotinin	1.75 Å	1P2M	1P2M	1P2M	1P2M	1P2M	1P2M	Helland et al., 2003
complex with aprotinin	1.80 Å	1P2N	1P2N	1P2N	1P2N	1P2N	1P2N	Helland et al., 2003
complex with aprotinin	2.00 Å	1P2O	1P2O	1P2O	1P2O	1P2O	1P2O	Helland et al., 2003
complex with aprotinin	1.80 Å	1P2Q	1P2Q	1P2Q	1P2Q	1P2Q	1P2Q	Helland et al., 2003
complex with aprotinin P1 Glu mutant	1.85 Å	1T7C	1T7C	1T7C	1T7C	1T7C	1T7C	Czapinska et al., 2004
complex with P1 Met mutant aprotinin	1.75 Å	1T8L	1T8L	1T8L	1T8L	1T8L	1T8L	Czapinska et al., 2004
complex with P1 His mutant aprotinin	1.80 Å	1T8M	1T8M	1T8M	1T8M	1T8M	1T8M	Czapinska et al., 2004
complex with P1 Thr mutant aprotinin	1.75 Å	1T8N	1T8N	1T8N	1T8N	1T8N	1T8N	Czapinska et al., 2004
complex with P1 Trp mutant aprotinin	1.70 Å	1T8O	1T8O	1T8O	1T8O	1T8O	1T8O	Czapinska et al., 2004
gamma-chymotrypsin; complex with L-para-chlorophenyl-1-acetamido boronic acid inhibitor	1.90 Å	1VGC	1VGC	1VGC	1VGC	1VGC	1VGC	Stoll et al., 1998
mature peptidase	1.34 Å	1YPH	1YPH	1YPH	1YPH	1YPH	1YPH
precursor	1.80 Å	2CGA	2CGA	2CGA	2CGA	2CGA	2CGA	Wang et al., 1985
alpha-chymotrypsin A	2.00 Å	2CHA	2CHA	2CHA	2CHA	2CHA	2CHA	Birktoft & Blow, 1972
gamma-chymotrypsin A	1.90 Å	2GCH	2GCH	2GCH	2GCH	2GCH	2GCH	Cohen et al., 1981
gamma-chymotrypsin A; pH 2.0	1.80 Å	2GCT	2GCT	2GCT	2GCT	2GCT	2GCT	Dixon et al., 1991
gamma-chymotrypsin A; complex with N-ac-L-Ala-L-Phe-chloroethylketone	1.80 Å	2GMT	2GMT	2GMT	2GMT	2GMT	2GMT	Kreutter et al., 1994
complex with benzohydroxamic acid/vanadate	1.50 Å	2P8O	2P8O	2P8O	2P8O	2P8O	2P8O	Moulin et al., 2007
gamma-chymotrypsin; complex with D-para-chloro-1-acetamido boronic acid inhibitor	1.80 Å	2VGC	2VGC	2VGC	2VGC	2VGC	2VGC	Stoll et al., 1998
mature peptidase	2.74 Å	2Y6T	2Y6T	2Y6T	2Y6T	2Y6T	2Y6T	Clark et al., 2011
complex with guamerin	2.50 Å	3BG4	3BG4	3BG4	3BG4	3BG4	3BG4	Kim et al., 2008
gamma-chymotrypsin B; complex with trans-O-hydroxy-alpha-methyl cinnamate	1.90 Å	3GCH	3GCH	3GCH	3GCH	3GCH	3GCH	Stoddard et al., 1990
gamma-chymotrypsin A; pH 10.5	1.60 Å	3GCT	3GCT	3GCT	3GCT	3GCT	3GCT	Dixon et al., 1991
mature peptidase	1.68 Å	3RU4	3RU4	3RU4	3RU4	3RU4	3RU4
mature peptidase	2.00 Å	3T62	3T62	3T62	3T62	3T62	3T62
gamma-chymotrypsin; complex with D-naphthyl-1-acetamido boronic acid inhibitor	1.67 Å	3VGC	3VGC	3VGC	3VGC	3VGC	3VGC	Stoll et al., 1998
alpha-chymotrypsin	1.68 Å	4CHA	4CHA	4CHA	4CHA	4CHA	4CHA	Tsukada & Blow, 1985
gamma-chymotrypsin; complex with diethylamino-O-hydroxy-alpha-methyl cinnamate	1.90 Å	4GCH	4GCH	4GCH	4GCH	4GCH	4GCH	Stoddard et al., 1990
mature peptidase	2.20 Å	4Q2K	4Q2K	4Q2K	4Q2K	4Q2K	4Q2K	Chua et al., 2014
gamma-chymotrypsin; complex with D-naphthyl-1-acetamido boronic acid inhibitor	2.10 Å	4VGC	4VGC	4VGC	4VGC	4VGC	4VGC	Stoll et al., 1998
alpha-chymotrypsin A	1.67 Å	5CHA	5CHA	5CHA	5CHA	5CHA	5CHA	Blevins & Tulinsky, 1985
photolysis product	2.70 Å	5GCH	5GCH	5GCH	5GCH	5GCH	5GCH	Stoddard et al., 1990
complex with bowman-birk inhibitor from soybean	2.30 Å	5J4Q	5J4Q	5J4Q	5J4Q	5J4Q	5J4Q
complex with a modified bowman-birk inhibitor from soybean	2.10 Å	5J4S	5J4S	5J4S	5J4S	5J4S	5J4S
alpha-chymotrypsin A; complex with phenylethane boronic acid	1.80 Å	6CHA	6CHA	6CHA	6CHA	6CHA	6CHA	Tulinsky & Blevins, 1987
crystal structure of bovine alpha-chymotrypsin in space group p65	1.86 Å	6DI8	6DI8	6DI8	6DI8	6DI8	6DI8
gamma-chymotrypsin; complex with N-Ac-L-Phe trifluoromethyl ketone	2.10 Å	6GCH	6GCH	6GCH	6GCH	6GCH	6GCH	Brady et al., 1990
gamma-chymotrypsin; complex with N-Ac-L-Leu-L-Phe trifluoromethyl ketone	1.80 Å	7GCH	7GCH	7GCH	7GCH	7GCH	7GCH	Brady et al., 1990
gamma-chymotrypsin; complex with Gly-Ala-Trp	1.60 Å	8GCH	8GCH	8GCH	8GCH	8GCH	8GCH	Harel et al., 1991