PDBsum entry 2gch

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protein Protein-protein interface(s) links
Hydrolase (serine proteinase) PDB id
Jmol PyMol
Protein chains
11 a.a.
131 a.a. *
95 a.a. *
Waters ×151
* Residue conservation analysis
PDB id:
Name: Hydrolase (serine proteinase)
Title: Refined crystal structure of gamma-chymotrypsin at 1.9 angst resolution
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:   0.181    
Authors: G.H.Cohen,D.R.Davies,E.W.Silverton
Key ref:
G.H.Cohen et al. (1981). Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases. J Mol Biol, 148, 449-479. PubMed id: 6914398 DOI: 10.1016/0022-2836(81)90186-8
21-May-80     Release date:   09-Jul-80    
Supersedes: 1gch
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

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     serine-type endopeptidase activity     1 term  


DOI no: 10.1016/0022-2836(81)90186-8 J Mol Biol 148:449-479 (1981)
PubMed id: 6914398  
Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases.
G.H.Cohen, E.W.Silverton, D.R.Davies.
No abstract given.

  Selected figure(s)  
Figure 1.
IG. . The progress of the partial refinement f tosyl-y-CHT nd, subsequently, native yCHT is shown. he left-hand curve refers to the osyl-y-CHT (2.7 ) and the right-hand one to the naive y-HT (1.9A). The refinement method is indicated along the horizontal bar in the igure sing the code: RS(m.i.r.). real-space mehod on .i.r. aps; S(ZF,-FJ. real-space method n 2F- F, aps; DDF, differential difference Fourier; Lt51, least-squares series 1; S2, least-squares series 2. The -factor is defined in the onventional manner as H = [[F,,[ - IF,II/x IF,], ere F, s an observed structure factor and F, is calculated tructure factor.
Figure 4.
FIG. 4. ntermolewlar nteractions in y-(`HI' bout the q-stallographic 4, axis n he vicinity fthr ac*tive cente. Residues of the nteracting molewles are distinguished bv using open and losed ckles. There are no lose ntermolecular contacts formed with he active-center residue. The ollowing intermolecular int,eractions denoted g thin ines) an e seen: ys90 N-sp64 61, ys90 N-(;11y59 0 and Phe41 0-Seti Oy. In addition, ater molecules 440 nd 54 form ridges between the 2 olecules.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1981, 148, 449-479) copyright 1981.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17912756 M.Shokhen, N.Khazanov, and A.Albeck (2008).
Screening of the active site from water by the incoming ligand triggers catalysis and inhibition in serine proteases.
  Proteins, 70, 1578-1587.  
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
17976015 C.A.Borgoño, J.A.Gavigan, J.Alves, B.Bowles, J.L.Harris, G.Sotiropoulou, and E.P.Diamandis (2007).
Defining the extended substrate specificity of kallikrein 1-related peptidases.
  Biol Chem, 388, 1215-1225.  
17600794 M.Shokhen, N.Khazanov, and A.Albeck (2007).
The cooperative effect between active site ionized groups and water desolvation controls the alteration of acid/base catalysis in serine proteases.
  Chembiochem, 8, 1416-1421.  
15557259 J.Mátrai, G.Verheyden, P.Krüger, and Y.Engelborghs (2004).
Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide.
  Protein Sci, 13, 3139-3150.  
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
11260254 K.Hara, M.Shiota, H.Kido, Y.Ohtsu, T.Kashiwagi, J.Iwahashi, N.Hamada, K.Mizoue, N.Tsumura, H.Kato, and T.Toyoda (2001).
Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site.
  Genes Cells, 6, 87-97.  
10617628 Y.Xu, A.Circolo, H.Jing, Y.Wang, S.V.Narayana, and J.E.Volanakis (2000).
Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding.
  J Biol Chem, 275, 378-385.  
10382669 A.Caputo, J.C.Parrish, M.N.James, J.C.Powers, and R.C.Bleackley (1999).
Electrostatic reversal of serine proteinase substrate specificity.
  Proteins, 35, 415-424.  
10024021 J.V.Lehtonen, K.Denessiouk, A.C.May, and M.S.Johnson (1999).
Finding local structural similarities among families of unrelated protein structures: a generic non-linear alignment algorithm.
  Proteins, 34, 341-355.  
  10422836 N.Armstrong, Lencastre, and E.Gouaux (1999).
A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase.
  Protein Sci, 8, 1475-1483.  
  9568890 A.R.Khan, and M.N.James (1998).
Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
  Protein Sci, 7, 815-836.  
  9508789 S.He, R.B.Sim, and K.Whaley (1998).
Mechanism of action of anti-C1-inhibitor autoantibodies: prevention of the formation of stable C1s-C1-inh complexes.
  Mol Med, 4, 119-128.  
  9232643 D.E.Timm (1997).
The crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme).
  Protein Sci, 6, 1418-1425.
PDB code: 1ao5
  8972386 G.W.Moss, J.Marshall, and E.Moczydlowski (1996).
Hypothesis for a serine proteinase-like domain at the COOH terminus of Slowpoke calcium-activated potassium channels.
  J Gen Physiol, 108, 473-484.  
7592653 S.Kim, S.V.Narayana, and J.E.Volanakis (1995).
Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.
  J Biol Chem, 270, 24399-24405.
PDB code: 1dst
7612659 T.Toyoguchi, K.Yamaguchi, S.Imajoh-Ohmi, N.Kato, M.Kusunoki, H.Kageyama, S.Sakiyama, S.Nagasawa, H.Moriya, and H.Sakiyama (1995).
Purification and characterization of recombinant hamster tissue complement C1s.
  Biochim Biophys Acta, 1250, 90-96.  
8086641 D.X.Hou, Y.Wang, H.Yamashita, S.Okamoto, K.Yokoyama, E.Soeda, and A.Sarai (1994).
Evolutionary conservation of chymotrypsinogen gene: genomic analysis and protein modeling.
  Jpn J Hum Genet, 39, 235-242.  
  8003958 Z.S.Hendsch, and B.Tidor (1994).
Do salt bridges stabilize proteins? A continuum electrostatic analysis.
  Protein Sci, 3, 211-226.  
8386628 B.Hinzmann, D.Wernicke, M.Pfeifer, U.Zacharias, B.Fischer, F.Eisenmenger, and H.Will (1993).
Tissue-type plasminogen activator mutants imitating urokinase in the peptide link between kringle and protease domains and at selected sites within the protease domain.
  Eur J Biochem, 213, 437-443.  
8332606 S.Nakagawa, H.A.Yu, M.Karplus, and H.Umeyama (1993).
Active site dynamics of acyl-chymotrypsin.
  Proteins, 16, 172-194.  
8281919 V.Dorovska-Taran, C.Veeger, and A.J.Visser (1993).
Reverse micelles as a water-property-control system to investigate the hydration/activity relationship of alpha-chymotrypsin.
  Eur J Biochem, 218, 1013-1019.  
1544459 A.V.Efimov (1992).
A novel super-secondary structure of beta-proteins. A triple-strand corner.
  FEBS Lett, 298, 261-265.  
1594574 J.A.Hartsuck, G.Koelsch, and S.J.Remington (1992).
The high-resolution crystal structure of porcine pepsinogen.
  Proteins, 13, 1.
PDB code: 3psg
1584778 L.Zhong, and W.C.Johnson (1992).
Environment affects amino acid preference for secondary structure.
  Proc Natl Acad Sci U S A, 89, 4462-4465.  
  1304349 W.Bode, D.Turk, and A.Karshikov (1992).
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships.
  Protein Sci, 1, 426-471.
PDB codes: 1ai8 1aix
1907667 J.Rose, and F.Eisenmenger (1991).
A fast unbiased comparison of protein structures by means of the Needleman-Wunsch algorithm.
  J Mol Evol, 32, 340-354.  
2381905 J.Greer (1990).
Comparative modeling methods: application to the family of the mammalian serine proteases.
  Proteins, 7, 317-334.  
2677049 J.S.Miller, E.H.Westin, and L.B.Schwartz (1989).
Cloning and characterization of complementary DNA for human tryptase.
  J Clin Invest, 84, 1188-1195.  
2622903 M.E.Karpen, Haseth, and K.E.Neet (1989).
Comparing short protein substructures by a method based on backbone torsion angles.
  Proteins, 6, 155-167.  
  2583108 W.Bode, I.Mayr, U.Baumann, R.Huber, S.R.Stone, and J.Hofsteenge (1989).
The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.
  EMBO J, 8, 3467-3475.
PDB code: 1ppb
  3366116 M.G.Grütter, G.Fendrich, R.Huber, and W.Bode (1988).
The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin.
  EMBO J, 7, 345-351.  
3448607 H.Iijima, J.B.Dunbar, and G.R.Marshall (1987).
Calibration of effective van der Waals atomic contact radii for proteins and peptides.
  Proteins, 2, 330-339.  
  3709526 C.Chothia, and A.M.Lesk (1986).
The relation between the divergence of sequence and structure in proteins.
  EMBO J, 5, 823-826.  
  3640709 W.Bode, A.Z.Wei, R.Huber, E.Meyer, J.Travis, and S.Neumann (1986).
X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.
  EMBO J, 5, 2453-2458.
PDB code: 1ppf
6877386 G.D.Rose, W.B.Young, and L.M.Gierasch (1983).
Interior turns in globular proteins.
  Nature, 304, 654-657.  
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.