PDBsum entry 1mtn

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protein ligands Protein-protein interface(s) links
Complex (hydrolase/inhibitor) PDB id
Protein chains
11 a.a.
131 a.a. *
97 a.a. *
58 a.a. *
SO4 ×4
Waters ×80
* Residue conservation analysis
PDB id:
Name: Complex (hydrolase/inhibitor)
Title: Bovine alpha-chymotrypsin:bpti crystallization
Structure: Alpha-chymotrypsin. Chain: a, e. Synonym: a-cht. Alpha-chymotrypsin. Chain: b, f. Synonym: a-cht. Alpha-chymotrypsin. Chain: c, g. Synonym: a-cht.
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas. Organ: pancreas
Biol. unit: Tetramer (from PQS)
2.80Å     R-factor:   0.180     R-free:   0.240
Authors: C.Capasso,M.Rizzi,E.Menegatti,P.Ascenzi,M.Bolognesi
Key ref: C.Capasso et al. (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. PubMed id: 9179777
28-Mar-96     Release date:   17-Aug-96    
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Protein chains
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
11 a.a.
Protein chains
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
131 a.a.
Protein chains
Pfam   ArchSchema ?
P00766  (CTRA_BOVIN) -  Chymotrypsinogen A
245 a.a.
97 a.a.
Protein chains
Pfam   ArchSchema ?
P00974  (BPT1_BOVIN) -  Pancreatic trypsin inhibitor
100 a.a.
58 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, 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     3 terms  


J Mol Recognit 10:26-35 (1997)
PubMed id: 9179777  
Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
C.Capasso, M.Rizzi, E.Menegatti, P.Ascenzi, M.Bolognesi.
The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved and refined at 2.8 A resolution (R-factor = 0.18). The proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is contacting both proteinase molecules in the dimer, through the reactive site loop and through residues next to the inhibitor's C-terminal region. Specific recognition between alpha-CHT and BPTI occurs at the (re)active site interface according to structural rules inferred from the analysis of homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being hydrogen bonded to backbone atoms of the enzyme surface residues Gly216 and Ser217.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20862438 F.Chiba, G.Mann, and L.J.Twyman (2010).
Investigating possible changes in protein structure during dendrimer-protein binding.
  Org Biomol Chem, 8, 5056-5058.  
19904357 J.Ohkanda, R.Satoh, and N.Kato (2009).
Protein surface recognition by dendritic ruthenium(II) tris(bipyridine) complexes.
  Chem Commun (Camb), (), 6949-6951.  
12581670 M.Laskowski, M.A.Qasim, and Z.Yi (2003).
Additivity-based prediction of equilibrium constants for some protein-protein associations.
  Curr Opin Struct Biol, 13, 130-139.  
11929986 N.O.Fischer, C.M.McIntosh, J.M.Simard, and V.M.Rotello (2002).
Inhibition of chymotrypsin through surface binding using nanoparticle-based receptors.
  Proc Natl Acad Sci U S A, 99, 5018-5023.  
11180535 D.J.Douglas, B.A.Collings, S.Numao, and V.J.Nesatyy (2001).
Detection of noncovalent complex between alpha-amylase and its microbial inhibitor tendamistat by electrospray ionization mass spectrometry.
  Rapid Commun Mass Spectrom, 15, 89-96.  
11151003 M.L.Lamb, K.W.Burdick, S.Toba, M.M.Young, A.G.Skillman, X.Zou, J.R.Arnold, and I.D.Kuntz (2001).
Design, docking, and evaluation of multiple libraries against multiple targets.
  Proteins, 42, 296-318.  
11523096 V.J.Nesatyy (2001).
Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry.
  J Mass Spectrom, 36, 950-959.  
  9925826 I.Favre, and E.Moczydlowski (1999).
Simultaneous binding of basic peptides at intracellular sites on a large conductance Ca2+-activated K+ channel. Equilibrium and kinetic basis of negatively coupled ligand interactions.
  J Gen Physiol, 113, 295-320.  
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