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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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PDB ID2est  sequence information (FASTA format)   
DescriptorELASTASE (E.C.3.4.21.11) COMPLEX WITH TRIFLUOROACETYL-L-LYSYL-L-ALANYL-P-TRIFLUOROMETHYLPHENYLANILIDE (TFAP)
TitleCRYSTALLOGRAPHIC STUDY OF THE BINDING OF A TRIFLUOROACETYL DIPEPTIDE ANILIDE INHIBITOR WITH ELASTASE
Functional KeywordsHYDROLASE (SERINE PROTEINASE)
Biological sourceSus scrofa (pig)
Cellular location [UNP - P00772] Secreted
Organ sourcePANCREAS
Total number of polymer chains2
Total molecular weight26481.7 (the details in Structural Details Page)
AuthorsSieker, L.C. , Hughes, D.L. (deposition date : 1986-03-24, release date : 1986-05-07)
Primary citationHughes, D.L. , Sieker, L.C. , Bieth, J. , Dimicoli, J.L.
Crystallographic study of the binding of a trifluoroacetyl dipeptide anilide inhibitor with elastase.
J. Mol. Biol., 162:645 - 658, 1982.(PubMed : 6926029)  (DOI: 10.1016/0022-2836(82)90393-X)
Experimental methodX-RAY DIFFRACTION ( 2.5[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00772 ) , eF-site , KEGG ( EC 3.4.21.36 ) , PISA