PDBsum entry 8gch

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protein ligands Protein-protein interface(s) links
Hydrolase/peptide PDB id
Protein chains
11 a.a.
131 a.a. *
96 a.a. *
SO4 ×4
Waters ×346
* Residue conservation analysis
PDB id:
Name: Hydrolase/peptide
Title: Gamma-chymotrypsin is a complex of alpha-chymotrypsin with i autolysis products
Structure: Gamma-chymotrypsin a. Chain: e. Gamma-chymotrypsin a. Chain: f. Gamma-chymotrypsin a. Chain: g. Gly ala trp peptide. Chain: c
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organism_taxid: 9913
1.60Å     R-factor:   0.193    
Authors: M.Harel,J.L.Sussman,I.Silman
Key ref:
M.Harel et al. (1991). Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products. Biochemistry, 30, 5217-5225. PubMed id: 2036388 DOI: 10.1021/bi00235a015
27-Mar-91     Release date:   15-Apr-92    
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.
96 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/bi00235a015 Biochemistry 30:5217-5225 (1991)
PubMed id: 2036388  
Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products.
M.Harel, C.T.Su, F.Frolow, I.Silman, J.L.Sussman.
The determination of three separate gamma-chymotrypsin structures at different temperatures and resolutions confirmed the presence of electron density in the active site, which could be interpreted as an oligopeptide as had previously been suggested by Dixon and Matthews [(1989) Biochemistry 28, 7033-7038]. HPLC analyses of the enzyme before and after crystallization demonstrated the presence of a wide variety of oligopeptides in the redissolved crystal, most with COOH-terminal aromatic residues, as expected of the products of chymotrypsin cleavage, which appeared to arise from extensive autolysis of the enzyme under the crystallization conditions. The refined structures agree well with the conformation of both gamma-chymotrypsin and alpha-chymotrypsin. The electron density in the active site is thus interpreted as arising from a repertoire of autolysed oligopeptides produced concomitantly with crystallization. The COOH-terminal carbons of the polypeptide(s) display short contact distances (1.97, 2.47, and 2.13 A, respectively) to Ser195 O gamma in all three refined structures, but the electron density is not continuous between these two atoms in any of them. This suggests that some sequences are covalently bound as enzyme intermediates while others are noncovalently bound as enzyme-product complexes.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18465087 P.Arun Prasad, and N.Gautham (2008).
A new peptide docking strategy using a mean field technique with mutually orthogonal Latin square sampling.
  J Comput Aided Mol Des, 22, 815-829.  
17909180 M.Debela, P.Hess, V.Magdolen, N.M.Schechter, T.Steiner, R.Huber, W.Bode, and P.Goettig (2007).
Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7.
  Proc Natl Acad Sci U S A, 104, 16086-16091.
PDB codes: 2qxg 2qxh 2qxi 2qxj
16754679 B.Liu, C.J.Schofield, and R.C.Wilmouth (2006).
Structural analyses on intermediates in serine protease catalysis.
  J Biol Chem, 281, 24024-24035.
PDB codes: 2bb4 2bd2 2bd3 2bd4 2bd5 2bd7 2bd8 2bd9 2bda 2bdb 2bdc 2h1u
16740631 M.Debela, V.Magdolen, N.Schechter, M.Valachova, F.Lottspeich, C.S.Craik, Y.Choe, W.Bode, and P.Goettig (2006).
Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences.
  J Biol Chem, 281, 25678-25688.  
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
12005439 B.M.Beadle, I.Trehan, P.J.Focia, and B.K.Shoichet (2002).
Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.
  Structure, 10, 413-424.
PDB codes: 1kvl 1kvm
12070326 C.Hetényi, and D.van der Spoel (2002).
Efficient docking of peptides to proteins without prior knowledge of the binding site.
  Protein Sci, 11, 1729-1737.  
12016211 F.X.Gomis-Rüth, A.Bayés, G.Sotiropoulou, G.Pampalakis, T.Tsetsenis, V.Villegas, F.X.Avilés, and M.Coll (2002).
The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family.
  J Biol Chem, 277, 27273-27281.
PDB code: 1gvl
12044569 I.J.Castellanos, G.Cruz, R.Crespo, and K.Griebenow (2002).
Encapsulation-induced aggregation and loss in activity of gamma-chymotrypsin and their prevention.
  J Control Release, 81, 307-319.  
11134922 W.R.Rypniewski, P.R.Ostergaard, M.Nørregaard-Madsen, M.Dauter, and K.S.Wilson (2001).
Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study of ligand binding.
  Acta Crystallogr D Biol Crystallogr, 57, 8.
PDB codes: 1fn8 1fy4 1fy5 1gdn 1gdq 1gdu
9914536 P.Hudáky, G.Kaslik, I.Venekei, and L.Gráf (1999).
The differential specificity of chymotrypsin A and B is determined by amino acid 226.
  Eur J Biochem, 259, 528-533.  
10380349 Y.Shimohigashi, T.Nose, Y.Yamauchi, and I.Maeda (1999).
Design of serine protease inhibitors with conformation restricted by amino acid side-chain-side-chain CH/pie interaction.
  Biopolymers, 51, 9.  
9733510 X.Wang, X.Lin, J.A.Loy, J.Tang, and X.C.Zhang (1998).
Crystal structure of the catalytic domain of human plasmin complexed with streptokinase.
  Science, 281, 1662-1665.
PDB code: 1bml
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
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