PDBsum entry 1cgj

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protein Protein-protein interface(s) links
Serine protease/inhibitor complex PDB id
Protein chains
245 a.a. *
56 a.a. *
Waters ×56
* Residue conservation analysis
PDB id:
Name: Serine protease/inhibitor complex
Title: Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (kazal-type)
Structure: Alpha-chymotrypsinogen. Chain: e. Engineered: yes. Pancreatic secretory trypsin inhibitor (kazal type) variant 4. Chain: i. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Homo sapiens. Human. Organism_taxid: 9606
Biol. unit: Dimer (from PQS)
2.30Å     R-factor:   0.195    
Authors: H.J.Hecht,M.Szardenings,J.Collins,D.Schomburg
Key ref: H.J.Hecht et al. (1991). Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type). J Mol Biol, 220, 711-722. PubMed id: 1870127
08-Oct-91     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
245 a.a.
Protein chain
Pfam   ArchSchema ?
P00995  (ISK1_HUMAN) -  Pancreatic secretory trypsin inhibitor
79 a.a.
56 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain E: 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!
  Cellular component     extracellular region   3 terms 
  Biological process     negative regulation of calcium ion import   9 terms 
  Biochemical function     catalytic activity     9 terms  


J Mol Biol 220:711-722 (1991)
PubMed id: 1870127  
Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type).
H.J.Hecht, M.Szardenings, J.Collins, D.Schomburg.
Variants of the human pancreatic secretory trypsin inhibitor (PSTI) have been created during a protein design project to generate a high-affinity inhibitor with respect to some serine proteases other than trypsin. Two modified versions of human PSTI with high affinity for chymotrypsin were crystallized as a complex with chymotrypsinogen. Both crystallize isomorphously in space group P4(1)2(1)2 with lattice constants a = 84.4 A, c = 86.7 A and diffract to 2.3 A resolution. The structure was solved by molecular replacement. The final R-value after refinement with 8.0 to 2.3 A resolution data was 19.5% for both complexes after inclusion of about 50 bound water molecules. The overall three-dimensional structure of PSTI is similar to the structure of porcine PSTI in the trypsinogen complex (1TGS). Small differences in the relative orientation of the binding loop and the core of the inhibitors indicate flexible adaptation to the proteases. The chymotrypsinogen part of the complex is similar to chymotrypsin. After refolding induced by binding of the inhibitor the root-mean-square difference of the active site residues A186 to A195 and A217 to A222 compared to chymotrypsin was 0.26 A.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18491388 J.Martin, L.Regad, C.Etchebest, and A.C.Camproux (2008).
Taking advantage of local structure descriptors to analyze interresidue contacts in protein structures and protein complexes.
  Proteins, 73, 672-689.  
16372349 K.Bastard, C.Prévost, and M.Zacharias (2006).
Accounting for loop flexibility during protein-protein docking.
  Proteins, 62, 956-969.  
11807947 L.Jiang, Y.Gao, F.Mao, Z.Liu, and L.Lai (2002).
Potential of mean force for protein-protein interaction studies.
  Proteins, 46, 190-196.  
11171964 S.M.Lu, W.Lu, M.A.Qasim, S.Anderson, I.Apostol, W.Ardelt, T.Bigler, Y.W.Chiang, J.Cook, M.N.James, I.Kato, C.Kelly, W.Kohr, T.Komiyama, T.Y.Lin, M.Ogawa, J.Otlewski, S.J.Park, S.Qasim, M.Ranjbar, M.Tashiro, N.Warne, H.Whatley, A.Wieczorek, M.Wieczorek, T.Wilusz, R.Wynn, W.Zhang, and M.Laskowski (2001).
Predicting the reactivity of proteins from their sequence alone: Kazal family of protein inhibitors of serine proteinases.
  Proc Natl Acad Sci U S A, 98, 1410-1415.  
10713514 A.Mac Sweeney, G.Birrane, M.A.Walsh, T.O'Connell, J.P.Malthouse, and T.M.Higgins (2000).
Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.
  Acta Crystallogr D Biol Crystallogr, 56, 280-286.
PDB code: 1dlk
10737939 D.W.Ritchie, and G.J.Kemp (2000).
Protein docking using spherical polar Fourier correlations.
  Proteins, 39, 178-194.  
10716920 G.Barbato, D.O.Cicero, F.Cordier, F.Narjes, B.Gerlach, S.Sambucini, S.Grzesiek, V.G.Matassa, R.De Francesco, and R.Bazzo (2000).
Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain.
  EMBO J, 19, 1195-1206.
PDB code: 1dxw
10944388 V.Z.Pletnev, T.S.Zamolodchikova, W.A.Pangborn, and W.L.Duax (2000).
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities.
  Proteins, 41, 8.
PDB code: 1euf
10328272 G.Moont, H.A.Gabb, and M.J.Sternberg (1999).
Use of pair potentials across protein interfaces in screening predicted docked complexes.
  Proteins, 35, 364-373.  
10022823 H.Jing, K.J.Macon, D.Moore, L.J.DeLucas, J.E.Volanakis, and S.V.Narayana (1999).
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.
  EMBO J, 18, 804-814.
PDB code: 1fdp
9179777 C.Capasso, M.Rizzi, E.Menegatti, P.Ascenzi, and M.Bolognesi (1997).
Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
  J Mol Recognit, 10, 26-35.
PDB code: 1mtn
8569452 P.Ascenzi, G.Amiconi, W.Bode, M.Bolognesi, M.Coletta, and E.Menegatti (1995).
Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: structural, functional and biomedical aspects.
  Mol Aspects Med, 16, 215-313.  
  8003977 C.L.Fisher, J.S.Greengard, and J.H.Griffin (1994).
Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen.
  Protein Sci, 3, 588-599.
PDB codes: 1pcu 2pct
1541261 W.Bode, and R.Huber (1992).
Natural protein proteinase inhibitors and their interaction with proteinases.
  Eur J Biochem, 204, 433-451.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.