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Serine protease inhibitor PDB id
1hpt
Jmol
Contents
Protein chain
56 a.a. *
Waters ×31
* Residue conservation analysis
PDB id:
1hpt
Name: Serine protease inhibitor
Title: Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (kazal type)
Structure: Pancreatic secretory trypsin inhibitor (kazal type) variant 3. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
2.30Å     R-factor:   0.191    
Authors: H.J.Hecht,M.Szardenings,J.Collins,D.Schomburg
Key ref: H.J.Hecht et al. (1992). Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal type). J Mol Biol, 225, 1095-1103. PubMed id: 1613792 DOI: 10.1016/0022-2836(92)90107-U
Date:
27-Mar-92     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biochemical function     protein binding     4 terms  

 

 
DOI no: 10.1016/0022-2836(92)90107-U J Mol Biol 225:1095-1103 (1992)
PubMed id: 1613792  
 
 
Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal type).
H.J.Hecht, M.Szardenings, J.Collins, D.Schomburg.
 
  ABSTRACT  
 
A modified version of the human pancreatic trypsin inhibitor (PSTI), generated in a protein-design project, has been crystallized in spacegroup P4(3) with lattice constants a = 40.15 A, c = 33.91 A. The structure has been solved by molecular replacement. Refinement of the structure by simulated annealing and conventional restrained least-squares yielded for 8.0 to 2.3 A data a final R-value of 19.1%. Differences to the known structures of porcine PSTI complexed with trypsinogen and modified human PSTI complexed with chymotrypsinogen occur at the flexible N-terminal part of the molecule. These differences are influenced by crystal packing, as are low temperature factors for the binding loop. The geometry of the binding loop is similar to the complexed structures.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20061306 S.Chaudhury, S.Lyskov, and J.J.Gray (2010).
PyRosetta: a script-based interface for implementing molecular modeling algorithms using Rosetta.
  Bioinformatics, 26, 689-691.  
17525091 O.Király, T.Wartmann, and M.Sahin-Tóth (2007).
Missense mutations in pancreatic secretory trypsin inhibitor (SPINK1) cause intracellular retention and degradation.
  Gut, 56, 1433-1438.  
14645103 C.W.Luo, H.J.Lin, S.C.Gopinath, and Y.H.Chen (2004).
Distinction of sperm-binding site and reactive site for trypsin inhibition on p12 secreted from the accessory sex glands of male mice.
  Biol Reprod, 70, 965-971.  
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.  
10737939 D.W.Ritchie, and G.J.Kemp (2000).
Protein docking using spherical polar Fourier correlations.
  Proteins, 39, 178-194.  
10737948 R.Najmanovich, J.Kuttner, V.Sobolev, and M.Edelman (2000).
Side-chain flexibility in proteins upon ligand binding.
  Proteins, 39, 261-268.  
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.  
9675278 J.Polanowska, I.Krokoszynska, H.Czapinska, W.Watorek, M.Dadlez, and J.Otlewski (1998).
Specificity of human cathepsin G.
  Biochim Biophys Acta, 1386, 189-198.  
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.