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Ligands
Code Name Style Show Link
0Z2 N-(trifluoroacetyl)-L-leucyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide
CA Calcium ion
DMF Dimethylformamide
SO4 Sulfate ion
Non-standard Residues
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Code : 7EST   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Interaction of the peptide CF3-LEU-ALA-NH-C6H4-CF3(TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 Angstroms
Release Data : 1991-10-15
Compound :
mol_id molecule chains
1 ELASTASE E
ec: 3.4.21.36
Source :
mol_id organism_scientific organism_common
1 Sus scrofa  (taxid:9823) Pig
organ: PANCREAS
Authors : Li De Lasierra, I., Prange, T.
Keywords : SERINE PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.8 Å )
Citation :

Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A.

de la Sierra, I.L.,Papamichael, E.,Sakarellos, C.  et al.
(1990)  J.Mol.Recog.  3 : 36 - 44

PubMed: 2354062
DOI: 10.1002/jmr.300030104

The Atomic Structure of Crystalline Porcine Pancreatic Elastase at 2.5 Angstroms Resolution. Comparisons with the Structure of Alpha-Chymotrypsin

Sawyer, L.,Shotton, C.M.,Campbell, J.W.  et al.
(1978)  J.Mol.Biol.  118 : 137

The Indirect Mechanism of Action of the Trifluoroacetyl Peptides on Elastase

Dimicoli, J.-L.,Renaud, A.,Bieth, J.
(1980)  Eur.J.Biochem.  107 : 423

Crystallographic Study of the Binding of a Tri-Fluoroacetyl Dipeptide Anilide Inhibitor with Elastase

Hughes, D.L.,Diecker, L.C.,Bieth, L.C.  et al.
(1982)  J.Mol.Biol.  162 : 645

Structure of native porcine pancreatic elastase at 1.65 A resolutions.

Meyer, E.,Cole, G.,Radhakrishnan, R.  et al.
(1988)  Acta Crystallogr B  44 ( Pt 1) : 26 - 38

PubMed: 3271103

Structure of the Product Complex of Acetyl-Ala-Pro-Ala with Porcine Pancreatic Elastase at 1.65 A Resolution

Meyer, E.,Radhakrishnan, R.,Cole, G.  et al.
(1986)  J.Mol.Biol.  189 : 533

Chain : E
UniProt : P00772 (CELA1_PIG)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa. 3.4.21.36 PubMed:5415108
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