PDBsum entry 1gct

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protein ligands Protein-protein interface(s) links
Hydrolase/peptide PDB id
Protein chains
11 a.a. *
131 a.a. *
95 a.a. *
Waters ×164
* Residue conservation analysis
PDB id:
Name: Hydrolase/peptide
Title: Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of g chymotrypsin?
Structure: Gamma-chymotrypsin a. Chain: a. Gamma-chymotrypsin a. Chain: b. Gamma-chymotrypsin a. Chain: c. Tetrapeptide adduct. Chain: d. Engineered: yes
Source: Bos taurus. Organism_taxid: 9913.
Biol. unit: Tetramer (from PQS)
1.60Å     R-factor:   0.173    
Authors: M.M.Dixon,B.W.Matthews
Key ref:
M.M.Dixon and B.W.Matthews (1989). Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin? Biochemistry, 28, 7033-7038. PubMed id: 2819046 DOI: 10.1021/bi00443a038
04-Sep-90     Release date:   15-Oct-91    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
11 a.a.
Protein chain
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
131 a.a.
Protein chain
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
95 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C: E.C.  - Chymotrypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     catalytic activity     2 terms  


DOI no: 10.1021/bi00443a038 Biochemistry 28:7033-7038 (1989)
PubMed id: 2819046  
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
M.M.Dixon, B.W.Matthews.
Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  19255494 W.R.Novak, A.G.Moulin, M.P.Blakeley, I.Schlichting, G.A.Petsko, and D.Ringe (2009).
A preliminary neutron diffraction study of gamma-chymotrypsin.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 317-320.  
17469803 A.Moulin, J.H.Bell, R.F.Pratt, and D.Ringe (2007).
Inhibition of chymotrypsin by a complex of ortho-vanadate and benzohydroxamic acid: structure of the inert complex and its mechanistic interpretation.
  Biochemistry, 46, 5982-5990.
PDB code: 2p8o
16636277 E.S.Radisky, J.M.Lee, C.J.Lu, and D.E.Koshland (2006).
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.
  Proc Natl Acad Sci U S A, 103, 6835-6840.
PDB codes: 2age 2agg 2agi 2ah4
15654893 N.Singh, T.Jabeen, S.Sharma, I.Roy, M.N.Gupta, S.Bilgrami, R.K.Somvanshi, S.Dey, M.Perbandt, C.Betzel, A.Srinivasan, and T.P.Singh (2005).
Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution.
  FEBS J, 272, 562-572.
PDB code: 1oxg
11080636 Y.Devedjiev, Z.Dauter, S.R.Kuznetsov, T.L.Jones, and Z.S.Derewenda (2000).
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.
  Structure, 8, 1137-1146.
PDB code: 1fj2
9718318 J.Lin, C.S.Cassidy, and P.A.Frey (1998).
Correlations of the basicity of His 57 with transition state analogue binding, substrate reactivity, and the strength of the low-barrier hydrogen bond in chymotrypsin.
  Biochemistry, 37, 11940-11948.  
9843946 J.Lin, W.M.Westler, W.W.Cleland, J.L.Markley, and P.A.Frey (1998).
Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin.
  Proc Natl Acad Sci U S A, 95, 14664-14668.  
9253409 L.Jin, B.A.Seaton, and J.F.Head (1997).
Crystal structure at 2.8 A resolution of anabolic ornithine transcarbamylase from Escherichia coli.
  Nat Struct Biol, 4, 622-625.
PDB code: 1akm
9188684 P.P.Berna, N.T.Mrabet, J.Van Beeumen, B.Devreese, J.Porath, and M.A.Vijayalakshmi (1997).
Residue accessibility, hydrogen bonding, and molecular recognition: metal-chelate probing of active site histidines in chymotrypsins.
  Biochemistry, 36, 6896-6905.  
9187653 R.C.Wilmouth, I.J.Clifton, C.V.Robinson, P.L.Roach, R.T.Aplin, N.J.Westwood, J.Hajdu, and C.J.Schofield (1997).
Structure of a specific acyl-enzyme complex formed between beta-casomorphin-7 and porcine pancreatic elastase.
  Nat Struct Biol, 4, 456-462.
PDB code: 1qix
8836107 C.M.Lukacs, J.Q.Zhong, M.I.Plotnick, H.Rubin, B.S.Cooperman, and D.W.Christianson (1996).
Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement.
  Nat Struct Biol, 3, 888-893.
PDB codes: 1ct3 2caa
8078901 D.Zhang, I.Botos, F.X.Gomis-Rüth, R.Doll, C.Blood, F.G.Njoroge, J.W.Fox, W.Bode, and E.F.Meyer (1994).
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
  Proc Natl Acad Sci U S A, 91, 8447-8451.
PDB codes: 1atl 1htd
8332606 S.Nakagawa, H.A.Yu, M.Karplus, and H.Umeyama (1993).
Active site dynamics of acyl-chymotrypsin.
  Proteins, 16, 172-194.  
2062832 B.L.Stoddard, P.Koenigs, N.Porter, K.Petratos, G.A.Petsko, and D.Ringe (1991).
Observation of the light-triggered binding of pyrone to chymotrypsin by Laue x-ray crystallography.
  Proc Natl Acad Sci U S A, 88, 5503-5507.  
2062826 J.A.Bell, K.P.Wilson, X.J.Zhang, H.R.Faber, H.Nicholson, and B.W.Matthews (1991).
Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
  Proteins, 10, 10-21.
PDB codes: 4lzm 5lzm 6lzm 7lzm
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