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PDBsum entry 1est
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Hydrolase PDB id
1est

 

 

 

 

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Contents
Protein chain
240 a.a. *
Ligands
SO4
TSU
Waters ×25
* Residue conservation analysis
PDB id:
1est
Name: Hydrolase
Title: The atomic structure of crystalline porcine pancreatic elastase at 2.5 angstroms resolution. Comparisons with the structure of alpha- chymotrypsin
Structure: Porcine pancreatic elastase. Chain: a. Engineered: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823
Resolution:
2.50Å     R-factor:   not given    
Authors: L.Sawyer,D.M.Shotton,H.C.Watson
Key ref:
L.Sawyer et al. (1978). The atomic structure of crystalline porcine pancreatic elastase at 2.5 A resolution: comparisons with the structure of alpha-chymotrypsin. J Mol Biol, 118, 137-208. PubMed id: 628010 DOI: 10.1016/0022-2836(78)90412-6
Date:
17-May-76     Release date:   27-May-76    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00772  (CELA1_PIG) -  Chymotrypsin-like elastase family member 1 from Sus scrofa
Seq:
Struc: 		266 a.a.
240 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.36  - pancreatic elastase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

 

 
DOI no: 10.1016/0022-2836(78)90412-6 J Mol Biol 118:137-208 (1978)
PubMed id: 628010  
 
 
The atomic structure of crystalline porcine pancreatic elastase at 2.5 A resolution: comparisons with the structure of alpha-chymotrypsin.
L.Sawyer, D.M.Shotton, J.W.Campbell, P.L.Wendell, H.Muirhead, H.C.Watson.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
FIG. 1. The variation in he ean arent and heavy-atom structure amplitudes and in he accurctcy of the hase etermination of the complete high resolution tosyl-elastse data set as a unction of sin20/ha. (-A-A-), F,//2 -O-O--), lfHl --m--W--, --O--O---, --A--/--) and E (-m-m--, -e-a--, -b-A-) are defined as in Tables 3 and 4. The values or wa are iven by the right ordinate, nd those or 1Frl, lfnl and E, which are n he same non-absolute scale, by the ordinate. A, CMBS-elastase; 0, ranyl tosyl-elastase; H, uranyl CMBS-elastase. 		Figure 10.
IG. 10. Histograms of (a) x, b) yz, (c) x3.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1978, 118, 137-208) copyright 1978.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16770643 B.Zhang, V.B.Tan, K.M.Lim, T.E.Tay, and S.Zhuang (2007).
Study of the inhibition of cyclin-dependent kinases with roscovitine and indirubin-3'-oxime from molecular dynamics simulations.
  J Mol Model, 13, 79-89.  
  17401204 T.Kinoshita, T.Tamada, K.Imai, K.Kurihara, T.Ohhara, T.Tada, and R.Kuroki (2007).
Crystallization of porcine pancreatic elastase and a preliminary neutron diffraction experiment.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 315-317.  
12198296 M.S.Weiss, S.Panjikar, E.Nowak, and P.A.Tucker (2002).
Metal binding to porcine pancreatic elastase: calcium or not calcium.
  Acta Crystallogr D Biol Crystallogr, 58, 1407-1412.
PDB codes: 1lka 1lkb
10707029 J.D.Szustakowski, and Z.Weng (2000).
Protein structure alignment using a genetic algorithm.
  Proteins, 38, 428-440.  
7846025 A.O.Smalås, E.S.Heimstad, A.Hordvik, N.P.Willassen, and R.Male (1994).
Cold adaption of enzymes: structural comparison between salmon and bovine trypsins.
  Proteins, 20, 149-166.
PDB code: 2tbs
7805627 R.W.Woody (1994).
Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins.
  Eur Biophys J, 23, 253-262.  
  1304887 E.Meyer (1992).
Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications.
  Protein Sci, 1, 1543-1562.  
1557349 J.S.Finer-Moore, A.A.Kossiakoff, J.H.Hurley, T.Earnest, and R.M.Stroud (1992).
Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction.
  Proteins, 12, 203-222.
PDB code: 5ptp
1438182 S.J.Prestrelski, D.M.Byler, and M.N.Liebman (1992).
Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlations in Fourier transform infrared spectroscopy.
  Proteins, 14, 440-450.  
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.  
2354062 I.L.de la Sierra, E.Papamichael, C.Sakarellos, J.L.Dimicoli, and T.Prangé (1990).
Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A.
  J Mol Recognit, 3, 36-44.
PDB codes: 6est 7est
2381905 J.Greer (1990).
Comparative modeling methods: application to the family of the mammalian serine proteases.
  Proteins, 7, 317-334.  
2662185 J.A.Sakanari, C.E.Staunton, A.E.Eakin, C.S.Craik, and J.H.McKerrow (1989).
Serine proteases from nematode and protozoan parasites: isolation of sequence homologs using generic molecular probes.
  Proc Natl Acad Sci U S A, 86, 4863-4867.  
2560195 J.S.Fetrow, T.S.Cardillo, and F.Sherman (1989).
Deletions and replacements of omega loops in yeast iso-1-cytochrome c.
  Proteins, 6, 372-381.  
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.  
  2469005 Y.Yun, and R.L.Davis (1989).
Levels of RNA from a family of putative serine protease genes are reduced in Drosophila melanogaster dunce mutants and are regulated by cyclic AMP.
  Mol Cell Biol, 9, 692-700.  
3228244 L.B.Evnin, and C.S.Craik (1988).
Development of an efficient method for generating and screening active trypsin and trypsin variants.
  Ann N Y Acad Sci, 542, 61-74.  
3273224 P.Ascenzi, M.Coletta, G.Amiconi, M.Bolognesi, M.Guarneri, and E.Menegatti (1988).
Zymogen activation: effect of peptides sequentially related to the bovine beta-trypsin N-terminus on Kazal inhibitor and benzamidine binding to bovine trypsinogen.
  J Mol Recognit, 1, 130-137.  
  3063392 S.R.Sprang, R.J.Fletterick, L.Gráf, W.J.Rutter, and C.S.Craik (1988).
Studies of specificity and catalysis in trypsin by structural analysis of site-directed mutants.
  Crit Rev Biotechnol, 8, 225-236.  
3553217 C.S.Craik, S.Roczniak, S.Sprang, R.Fletterick, and W.Rutter (1987).
Redesigning trypsin via genetic engineering.
  J Cell Biochem, 33, 199-211.  
3663857 L.G.Presta, and E.F.Meyer (1987).
Prediction of protein--ligand interactions: the complex of porcine pancreatic elastase with a valine-derived benzoxazinone.
  Biopolymers, 26, 1207-1225.  
3663854 M.C.Manning, and R.W.Woody (1987).
Theoretical determination of the CD of proteins containing closely packed antiparallel beta-sheets.
  Biopolymers, 26, 1731-1752.  
3636229 B.Kerfelec, C.Cambillau, A.Puigserver, and C.Chapus (1986).
The inactive subunit of ruminant procarboxypeptidase A-S6 complexes. Structural basis of inactivity and physiological role.
  Eur J Biochem, 157, 531-538.  
3333471 M.A.Norcross (1986).
Models for MHC-restricted T-cell antigen recognition.
  Bioessays, 5, 153-157.  
3519215 N.Venot, M.Sciaky, A.Puigserver, P.Desnuelle, and G.Laurent (1986).
Amino acid sequence and disulfide bridges of subunit III, a defective endopeptidase present in the bovine pancreatic 6 S procarboxypeptidase A complex.
  Eur J Biochem, 157, 91-99.  
  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
7032913 C.A.Bauer, G.D.Brayer, A.R.Sielecki, and M.N.James (1981).
Active site of alpha-lytic protease: enzyme-substrate interactions.
  Eur J Biochem, 120, 289-294.  
7038675 W.W.Bachovchin, R.Kaiser, J.H.Richards, and J.D.Roberts (1981).
Catalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease.
  Proc Natl Acad Sci U S A, 78, 7323-7326.  
6910426 C.Ghélis (1980).
Transient conformational states in proteins followed by differential labeling.
  Biophys J, 32, 503-514.  
284382 C.V.Glover, and M.A.Gorovsky (1979).
Amino-acid sequence of Tetrahymena histone H4 differs from that of higher eukaryotes.
  Proc Natl Acad Sci U S A, 76, 585-589.  
262424 P.Y.Chou, and G.D.Fasman (1979).
Conservation of chain reversal regions in proteins.
  Biophys J, 26, 385-399.  
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 codes are shown on the right.

 

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