PDBsum entry 4gch

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Hydrolase (serine proteinase) PDB id
Protein chains
11 a.a.
131 a.a. *
95 a.a. *
Waters ×73
* Residue conservation analysis
PDB id:
Name: Hydrolase (serine proteinase)
Title: Structure and activity of two photoreversible cinnamates bou chymotrypsin
Structure: Gamma-chymotrypsin a. Chain: e. Gamma-chymotrypsin a. Chain: f. Gamma-chymotrypsin a. Chain: g. Ec:
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913
Biol. unit: Trimer (from PQS)
1.90Å     R-factor:   0.209    
Authors: B.L.Stoddard,D.Ringe,G.A.Petsko
Key ref:
B.L.Stoddard et al. (1990). Structure and activity of two photoreversible cinnamates bound to chymotrypsin. Biochemistry, 29, 4871-4879. PubMed id: 2364065 DOI: 10.1021/bi00472a017
25-Sep-89     Release date:   15-Oct-90    
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 E, F, G: 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/bi00472a017 Biochemistry 29:4871-4879 (1990)
PubMed id: 2364065  
Structure and activity of two photoreversible cinnamates bound to chymotrypsin.
B.L.Stoddard, J.Bruhnke, N.Porter, D.Ringe, G.A.Petsko.
The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.

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.  
11327865 D.Neidhart, Y.Wei, C.Cassidy, J.Lin, W.W.Cleland, and P.A.Frey (2001).
Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin.
  Biochemistry, 40, 2439-2447.
PDB codes: 1gg6 1ggd
12203645 K.Zou, W.T.Miller, R.S.Givens, and H.Bayley (2001).
Caged Thiophosphotyrosine Peptides.
  Angew Chem Int Ed Engl, 40, 3049-3051.  
9578548 M.P.Weir, S.S.Bethell, A.Cleasby, C.J.Campbell, R.J.Dennis, C.J.Dix, H.Finch, H.Jhoti, C.J.Mooney, S.Patel, C.M.Tang, M.Ward, A.J.Wonacott, and C.W.Wharton (1998).
Novel natural product 5,5-trans-lactone inhibitors of human alpha-thrombin: mechanism of action and structural studies.
  Biochemistry, 37, 6645-6657.
PDB codes: 1awf 1awh
8888067 B.L.Stoddard (1996).
Intermediate trapping and laue X-ray diffraction: potential for enzyme mechanism, dynamics, and inhibitor screening.
  Pharmacol Ther, 70, 215-256.  
1583540 H.J.Böhm (1992).
The computer program LUDI: a new method for the de novo design of enzyme inhibitors.
  J Comput Aided Mol Des, 6, 61-78.  
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.  
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