_EC 3.4.21.1 chymotrypsin.

94 PDB entries

EC 3.-.-.- Hydrolases. [51,952 PDB entries] EC 3.4.-.- Acting on peptide bonds (peptidases). [15,916 PDB entries] EC 3.4.21.- Serine endopeptidases. [4,998 PDB entries] EC 3.4.21.1 chymotrypsin. [94 PDB entries]

1ab9

Reaction:		Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Other name(s):		alpha-chymotrypsin. chymotrypsin A. chymotrypsin B.
Comments:		Belongs to peptidase family S1. Formerly Ec 3.4.4.5 and Ec 3.4.4.6.
Links:		[IntEnz]   [ExPASy]   [KEGG]

There are 94 PDB entries in enzyme class E.C.3.4.21.1

PDB code		Protein
1ab9		Crystal structure of bovine gamma-chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Chains: B, C (131 residues) CATH domain: 2.40.10.10
1acb		Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 angstroms resolution Source: Bos taurus. Bovine. Organism_taxid: 9913. Hirudo medicinalis. Medicinal leech. Organism_taxid: 6421 Chain: E (241 residues) CATH domains: 2.40.10.10 2.40.10.10
1afq		Crystal structure of bovine gamma-chymotrypsin complexed with a synthetic inhibitor Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
1ca0		Bovine chymotrypsin complexed to appi Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreatic. Gene: a4. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Chains: A, B, C, F, G, H (11 residues)
1cbw		Bovine chymotrypsin complexed to bpti Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas Chains: A, B, C, F, G, H (11 residues)
1cgi		Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (kazal-type) Source: Bos taurus. Cattle. Organism_taxid: 9913. Homo sapiens. Human. Organism_taxid: 9606 Chain: E (245 residues) CATH domains: 2.40.10.10 2.40.10.10
1cgj		Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (kazal-type) Source: Bos taurus. Cattle. Organism_taxid: 9913. Homo sapiens. Human. Organism_taxid: 9606 Chain: E (245 residues) CATH domains: 2.40.10.10 2.40.10.10
1chg		Chymotrypsinogen,2.5 angstroms crystal structure, comparison with alpha-chymotrypsin,and implications for zymogen activation Source: Bos taurus. Cattle. Organism_taxid: 9913 Chain: A (230 residues) CATH domains: 2.40.10.10 2.40.10.10
1cho		Crystal and molecular structures of the complex of alpha- Chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913. Meleagris gallopavo. Turkey. Organism_taxid: 9103 Chains: F, G (131 residues) CATH domain: 2.40.10.10
1dlk		Crystal structure analysis of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Synthetic: yes. Other_details: this sequence was synthetically constructed Chains: A, B, C, D (13 residues)
1eq9		Crystal structure of fire ant chymotrypsin complexed to pmsf Source: Solenopsis invicta. Red fire ant. Organism_taxid: 13686 Chains: A, B (222 residues) CATH domains: 2.40.10.10 2.40.10.10
1ex3		Crystal structure of bovine chymotrypsinogen a (tetragonal) Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas Chain: A (245 residues) CATH domains: 2.40.10.10 2.40.10.10
1gcd		Refined crystal structure of "aged" and "non-aged" organophosphoryl conjugates of gamma-chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913 Chain: A (237 residues) CATH domains: 2.40.10.10 2.40.10.10
1gct		Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of gamma- chymotrypsin? Source: Bos taurus. Organism_taxid: 9913. Chains: A, B, C (11 residues)
1gg6		Crystal structure of gamma chymotrypsin with n-acetyl-phenylalanine trifluoromethyl ketone bound at the active site Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
1ggd		Crystal structure of gamma chymotrypsin with n-acetyl-leucil- phenylalanine aldehyde bound at the active site Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
1gha		A second active site in chymotrypsin? the x-ray crystal structure of n-acetyl-d-tryptophan bound to gamma-chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Chains: E, F, G (11 residues)
1ghb		A second active site in chymotrypsin? the x-ray crystal structure of n-acetyl-d-tryptophan bound to gamma-chymotrypsin Source: Bos taurus. Organism_taxid: 9913. Chains: E, F, G (11 residues)
1gl0		Structure of the complex between bovine alpha-chymotrypsin and pmp- d2v, an inhibitor from the insect locusta migratoria Source: Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas. Synthetic: yes. Locusta migratoria. Migratory locust. Organism_taxid: 7004 Chain: E (241 residues) CATH domains: 2.40.10.10 2.40.10.10
1gl1		Structure of the complex between bovine alpha-chymotrypsin and pmp-c, an inhibitor from the insect locusta migratoria Source: Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas. Synthetic: yes. Locusta migratoria. Migratory locust. Organism_taxid: 7004 Chains: A, B, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1gmc		The x-ray crystal structure of the tetrahedral intermediate of gamma- chymotrypsin in hexane Source: Bos taurus. Cattle. Organism_taxid: 9913. Chains: E, F, G (11 residues)
1gmd		X-ray crystal structure of gamma-chymotrypsin in hexane Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
1gmh		Refined crystal structure of "aged" and "non-aged" organophosphoryl conjugates of gamma-chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: F, G (131 residues) CATH domain: 2.40.10.10
1hja		Lys 18 variant of turkey ovomucoid inhibitor third domain complexed with alpha-chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Other_details: commercial product of worthington biochemical corporation. Expressed in: escherichia coli. Expression_system_taxid: 562. Meleagris gallopavo. Turkey. Chains: B, C (131 residues) CATH domain: 2.40.10.10
1k2i		Crystal structure of gamma-chymotrypsin in complex with 7- hydroxycoumarin Source: Bos taurus. Cattle. Organism_taxid: 9913 Chain: 1 (236 residues) CATH domains: 2.40.10.10 2.40.10.10
1kdq		Crystal structure analysis of the mutant s189d rat chymotrypsin Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Chains: A, B (130 residues) CATH domain: 2.40.10.10
1mtn		Bovine alpha-chymotrypsin:bpti crystallization Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: A, B, C, E, F, G (11 residues)
1n8o		Crystal structure of a complex between bovine chymotrypsin and ecotin Source: Bos taurus. Cattle. Organism_taxid: 9913. Escherichia coli. Organism_taxid: 83333. Strain: k12 Chains: A, B, C (11 residues)
1oxg		Crystal structure of a complex formed between organic solvent treated bovine alpha-chymotrypsin and its autocatalytically produced highly potent 14-residue peptide at 2.2 resolution Source: Bos taurus. Bovine. Organism_taxid: 9913. Secretion: pancreatic secretion. Secretion: pancreatic secretion Chains: A, B (241 residues) CATH domains: 2.40.10.10 2.40.10.10
1p2m		Structural consequences of accommodation of four non-cognate amino- acid residues in the s1 pocket of bovine trypsin and chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: t7 promoter Chains: A, C (238 residues) CATH domains: 2.40.10.10 2.40.10.10
1p2n		Structural consequences of accommodation of four non-cognate amino- acid residues in the s1 pocket of bovine trypsin and chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: t7 promoter Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1p2o		Structural consequences of accommodation of four non-cognate amino- acid residues in the s1 pocket of bovine trypsin and chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: t7 promoter Chains: A, C (238 residues) CATH domains: 2.40.10.10 2.40.10.10
1p2q		Structural consequences of accommodation of four non-cognate amino- acid residues in the s1 pocket of bovine trypsin and chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: t7 promoter Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1t7c		Crystal structure of the p1 glu bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1t8l		Crystal structure of the p1 met bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1t8m		Crystal structure of the p1 his bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1t8n		Crystal structure of the p1 thr bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1t8o		Crystal structure of the p1 trp bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, C (239 residues) CATH domains: 2.40.10.10 2.40.10.10
1vgc		Gamma-chymotrypsin l-para-chloro-1-acetamido boronic acid inhibitor complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
1yph		High resolution structure of bovine alpha-chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: C, E, B, D, F (131 residues) CATH domain: 2.40.10.10
2cga		Bovine chymotrypsinogen a. X-ray crystal structure analysis and refinement of a new crystal form at 1.8 angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913 Chains: A, B (245 residues) CATH domains: 2.40.10.10 2.40.10.10
2cha		The structure of crystalline alpha-chymotrypsin, v.The atomic structure of tosyl-alpha-chymotrypsin at 2 angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C, F, G (131 residues) CATH domain: 2.40.10.10
2gch		Refined crystal structure of gamma-chymotrypsin at 1.9 angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
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 Source: Bos taurus. Organism_taxid: 9913. Chains: A, B, C (11 residues)
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 Source: Bos taurus. Cattle. Organism_taxid: 9913. Chains: B, C (131 residues) CATH domain: 2.40.10.10
2jet		Crystal structure of a trypsin-like mutant (s189d , a226g) chymotrypsin. Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Organ: pancreas. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C (12 residues)
2p8o		Crystal structure of a benzohydroxamic acid/vanadate complex bound to chymotrypsin a Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues) CATH domain: 2.40.10.10
2vgc		Gamma-chymotrypsin d-para-chloro-1-acetamido boronic acid inhibitor complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
2y6t		Molecular recognition of chymotrypsin by the serine protease inhibitor ecotin from yersinia pestis Source: Bos taurus. Cattle. Organism_taxid: 9913. Other_details: activated bovine chymotrypsin was purchased from sigma-aldrich. Yersinia pseudotuberculosis. Organism_taxid: 502800. Strain: ypiii. Expressed in: escherichia coli. Chains: A, B, C, D (240 residues) CATH domains: 2.40.10.10 2.40.10.10
3bg4		The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor Source: Bos taurus. Bovine. Organism_taxid: 9913. Hirudo nipponia. Leech. Organism_taxid: 42736. Expressed in: pichia pastoris. Expression_system_taxid: 4922 Chains: A, B, C (11 residues)
3cp7		Crystal structure of a thermostable serine protease al20 from extremophilic microoganism Source: Nesterenkonia abyssinica Chains: A, B (216 residues) CATH domains: 2.40.10.10 2.40.10.10 6.10.250.400
3gch		Chemistry of caged enzymes. Binding of photoreversible cinnamates to chymotrypsin Source: Bos taurus. Bos taurus Chains: A, B, C (11 residues)
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 Source: Bos taurus. Cattle. Organism_taxid: 9913. Chains: E, F, G (11 residues)
3ru4		Crystal structure of the bowman-birk serine protease inhibitor btci in complex with trypsin and chymotrypsin Source: Bos taurus. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913. Vigna unguiculata. Cowpea. Organism_taxid: 3917. Organism_taxid: 9913 Chains: C, D, E (11 residues)
3t62		Crystal structure of recombinant kunitz type serine protease inhibitor-1 from the caribbean sea anemone stichodactyla helianthus in complex with bovine chymotrypsin Source: Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas. Stichodactyla helianthus. Caribbean sea anemone. Organism_taxid: 6123. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Chains: A, B, C (240 residues) CATH domains: 2.40.10.10 2.40.10.10
3vgc		Gamma-chymotrypsin l-naphthyl-1-acetamido boronic acid acid inhibitor complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
3wy8		Crystal structure of protease anisep from arthrobacter nicotinovorans Source: Arthrobacter nicotinovorans. Organism_taxid: 29320. Strain: 23-0-11. Gene: spr. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (219 residues) CATH domains: 2.40.10.10 2.40.10.10
4cha		Structure of alpha- Chymotrypsin refined at 1.68 angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: A, B, C, F, G (11 residues)
4gch		Structure and activity of two photoreversible cinnamates bound to chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
4q2k		Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5b Source: Bos taurus. Bovine. Organism_taxid: 9913 Chains: A, B, C, D (231 residues) CATH domains: 2.40.10.10 2.40.10.10
4vgc		Gamma-chymotrypsin d-naphthyl-1-acetamido boronic acid inhibitor complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: B, C (131 residues) CATH domain: 2.40.10.10
5cha		The refinement and the structure of the dimer of alpha- Chymotrypsin at 1.67- Angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C, F, G (131 residues) CATH domain: 2.40.10.10
5gch		Chemistry of caged enzymes II . Photoactivation of inhibited chymotrypsin Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
5j4q		Alpha-chymotrypsin from bovine pancreas in complex with bowman-birk inhibitor from soybean Source: Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas. Glycine max. Soybean. Organism_taxid: 3847 Chain: A (241 residues) CATH domains: 2.40.10.10 2.40.10.10
5j4s		Alpha-chymotrypsin from bovine pancreas in complex with a modified bowman-birk inhibitor from soybean Source: Bos taurus. Bovine. Organism_taxid: 9913. Synthetic: yes. Glycine max. Soybean. Organism_taxid: 3847 Chain: A (241 residues) CATH domains: 2.40.10.10 2.40.10.10
5r42		Crystal structure of deuterated gamma-chymotrypsin at ph 7.5, room temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r43		Crystal structure of deuterated gamma-chymotrypsin at ph 7.5, cryo temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r44		Crystal structure of gamma-chymotrypsin at ph 7.5, room temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r45		Crystal structure of gamma-chymotrypsin at ph 7.5, cryo temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r46		Crystal structure of deuterated gamma-chymotrypsin at ph 5.6, room temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r47		Crystal structure of deuterated gamma-chymotrypsin at ph 5.6, cryo temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r48		Crystal structure of gamma-chymotrypsin at ph 5.6, room temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r49		Crystal structure of gamma-chymotrypsin at ph 5.6, cryo temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r4a		Crystal structure of deuterated gamma-chymotrypsin at ph 9, room temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r4b		Crystal structure of deuterated gamma-chymotrypsin at ph 9, cryo temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r4c		Crystal structure of gamma-chymotrypsin at ph 9, room temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
5r4d		Crystal structure of gamma-chymotrypsin at ph 9, cryo temperature Source: Bos taurus. Bovine. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C (131 residues)
6cha		Structure of a tetrahedral transition state complex of alpha- Chymotrypsin at 1.8- Angstroms resolution Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: B, C, F, G (131 residues) CATH domain: 2.40.10.10
6di8		Crystal structure of bovine alpha-chymotrypsin in space group p65 Source: Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas Chains: A, B, C, D, E, F, G, H, I, J, K, L (13 residues)
6gch		Structure of chymotrypsin- Trifluoromethyl ketone inhibitor complexes. Comparison of slowly and rapidly equilibrating inhibitors Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
7gch		Structure of chymotrypsin- Trifluoromethyl ketone inhibitor complexes. Comparison of slowly and rapidly equilibrating inhibitors Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
7jrx		Crystal structure of the r64f mutant of bauhinia bauhinioides complexed with bovine chymotrypsin Source: Bos taurus. Bovine. Organism_taxid: 9913. Bauhinia bauhinioides. Organism_taxid: 166014. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B, C, a, b, c (13 residues)
7kty		Data clustering and dynamics of chymotrypsinogen average structure Source: Bos taurus. Bovine. Organism_taxid: 9913 Chain: A (241 residues)
7ktz		Data clustering and dynamics of chymotrypsinogen cluster 131 (purple) structure Source: Bos taurus. Bovine. Organism_taxid: 9913 Chain: A (241 residues)
7ku0		Data clustering and dynamics of chymotrypsinogen cluster 138 (yellow) structure Source: Bos taurus. Bovine. Organism_taxid: 9913 Chain: A (241 residues)
7ku1		Data clustering and dynamics of chymotrypsinogen cluster 139 (green) structure Source: Bos taurus. Bovine. Organism_taxid: 9913 Chain: A (241 residues)
7ku2		Data clustering and dynamics of chymotrypsinogen clulster 140 (structure) Source: Bos taurus. Bovine. Organism_taxid: 9913 Chain: A (241 residues)
7ku3		Data clustering and dynamics of chymotrypsinogen cluster 141 (cyan) structure Source: Bos taurus. Bovine. Organism_taxid: 9913 Chain: A (241 residues)
7qiq		Crystal structure of the p1 aminobutanoic acid (abu) bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Synthetic: yes. Organism_taxid: 9913 Chains: A, B, C, E, F, G (11 residues)
7qir		Crystal structure of the p1 monofluorethylglycine(mfegly) bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Synthetic: yes. Organism_taxid: 9913 Chains: A, B, C, E, F, G (11 residues)
7qis		Crystal structure of the p1 difluoroethylglycine (dfegly) bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Synthetic: yes. Organism_taxid: 9913 Chains: A, B, C, E, F, G (12 residues)
7qit		Crystal structure of the p1 trifluoroethylglycine (tfegly) bpti mutant- bovine chymotrypsin complex Source: Bos taurus. Cattle. Organism_taxid: 9913. Synthetic: yes. Organism_taxid: 9913 Chains: A, B, C, E, F, G (11 residues)
8gch		Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913 Chains: E, F, G (11 residues)
9f6h		Crystal structure of bovine alpha-chymotrypsin in complex with the bicyclic peptide inhibitor mp5.4.3 Source: Bos taurus. Cattle. Organism_taxid: 9913. Synthetic: yes. Synthetic construct. Organism_taxid: 32630 Chains: A, B, C (13 residues)