PDBsum entry 9api

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Proteinase inhibitor PDB id
Protein chains
339 a.a. *
36 a.a. *
* Residue conservation analysis
PDB id:
Name: Proteinase inhibitor
Title: The s variant of human alpha1-antitrypsin, structure and imp for function and metabolism
Structure: Alpha 1-antitrypsin. Chain: a. Engineered: yes. Alpha 1-antitrypsin. Chain: b. Engineered: yes
Source: not given
Biol. unit: Dimer (from PQS)
3.00Å     R-factor:   0.209    
Authors: H.Loebermann,R.Tokuoka,J.Deisenhofer,R.Huber
Key ref: R.Engh et al. (1989). The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism. Protein Eng, 2, 407-415. PubMed id: 2785270
08-Sep-88     Release date:   15-Oct-90    
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Protein chain
Pfam   ArchSchema ?
P01009  (A1AT_HUMAN) -  Alpha-1-antitrypsin
418 a.a.
339 a.a.
Protein chain
Pfam   ArchSchema ?
P01009  (A1AT_HUMAN) -  Alpha-1-antitrypsin
418 a.a.
36 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


Protein Eng 2:407-415 (1989)
PubMed id: 2785270  
The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism.
R.Engh, H.Löbermann, M.Schneider, G.Wiegand, R.Huber, C.B.Laurell.
The S variant of the human alpha 1-antitrypsin with E-264----V, is responsible for a mild alpha 1-antitrypsin deficiency quite common in the European population. S protein specifically cleaved at the susceptible peptide bond was crystallized and its crystal structure determined and refined to 3.1 A resolution. The S variant crystallizes isomorphous to the normal M variant. The difference Fourier electron density map shows the E----V change as outstanding residual density. In addition, small structural changes of the main polypeptide chain radiate from the site of mutation and affect parts far removed from it. By the mutation, internal hydrogen bonds and salt linkages of E-264 to Y-38 and K-487, respectively, are lost. They cause the far-reaching slight distortions and are probably related to the reduced thermal stability of the S mutant. They may also be responsible for slower folding of the polypeptide chain and the clinical symptoms of alpha 1-antitrypsin deficiency. In a theoretical study by molecular dynamics methods simulations of the M and S proteins were made and the results analysed with respect to structural and dynamic properties and compared with the experimental results. There is a significant correlation between experimental and theoretical results in some respects.

Literature references that cite this PDB file's key reference

  PubMed id Reference
16698543 M.J.Bennett, M.R.Sawaya, and D.Eisenberg (2006).
Deposition diseases and 3D domain swapping.
  Structure, 14, 811-824.  
12694181 T.Wind, J.K.Jensen, D.M.Dupont, P.Kulig, and P.A.Andreasen (2003).
Mutational analysis of plasminogen activator inhibitor-1.
  Eur J Biochem, 270, 1680-1688.  
  10933492 P.R.Elliott, X.Y.Pei, T.R.Dafforn, and D.A.Lomas (2000).
Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease.
  Protein Sci, 9, 1274-1281.
PDB code: 1qlp
8901864 P.R.Elliott, P.E.Stein, D.Bilton, R.W.Carrell, and D.A.Lomas (1996).
Structural explanation for the deficiency of S alpha 1-antitrypsin.
  Nat Struct Biol, 3, 910-911.  
  8401226 T.Samandari, and J.L.Brown (1993).
A study of the effects of altering the sites for N-glycosylation in alpha-1-proteinase inhibitor variants M and S.
  Protein Sci, 2, 1400-1410.  
1541261 W.Bode, and R.Huber (1992).
Natural protein proteinase inhibitors and their interaction with proteinases.
  Eur J Biochem, 204, 433-451.  
  2247868 N.Kalsheker, and K.Morgan (1990).
Molecular biology and respiratory disease. 7. The alpha 1 antitrypsin gene and chronic lung disease.
  Thorax, 45, 759-764.  
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