PDBsum entry 1eld

Hydrolase/hydrolase inhibitor

PDB id: 1eld

Contents

Protein chain

240 a.a. *

Ligands

0Z0

ACY

Metals

_CA

Waters ×133

* Residue conservation analysis

PDB id:

1eld

Name:

Hydrolase/hydrolase inhibitor

Title:

Structural analysis of the active site of porcine pancreatic elastase based on the x-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors

Structure:

Elastase. Chain: e. Engineered: yes

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organ: pancreas

Resolution:

2.00Å R-factor: 0.196

Authors:

C.Mattos,G.A.Petsko,D.Ringe

Key ref:

C.Mattos et al. (1995). Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors. Biochemistry, 34, 3193-3203. PubMed id: 7880814 DOI: 10.1021/bi00010a008

Date:

24-Oct-94 Release date: 14-Feb-95

Protein chain

P00772  (CELA1_PIG) -  Chymotrypsin-like elastase family member 1 from Sus scrofa

Seq: 266 a.a.

Struc: 240 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.21.36 - pancreatic elastase.
• Reaction: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

DOI no: 10.1021/bi00010a008

Biochemistry 34:3193-3203 (1995)

PubMed id: 7880814

Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.

C.Mattos, D.A.Giammona, G.A.Petsko, D.Ringe.

ABSTRACT

The X-ray crystal structures of two new (trifluoroacetyl)dipeptide p-(trifluoromethyl)anilide (TFA-dipeptide-TFM) inhibitors complexed to porcine pancreatic elastase are presented. TFA-Val-Ala-TFM and TFA-Phe-Ala-TFM both bind to elastase with the TFA group in the S1 subsite, Val or Phe in the S2 subsite, Ala in the S3 subsite, and the TFM group in the S4 subsite. Five other TFA-dipeptide-anilide/elastase crystal structures are available (two TFA-X-Ala-p-(trifluoromethyl)anilide, X = Lys, Leu, and three TFA-Lys-X-p-isopropylanilide, X = Pro, Leu, Phe). The four inhibitors with the trifluoromethyl substituent on the anilide ring bind in a single mode to elastase, whereas superposition of the three inhibitors with the isopropyl substituent on the anilide ring show three different modes of binding to the protein [Mattos, C., et al. (1994) Nature Struct. Biol. 1, 55-58]. The seven structures are taken together in a detailed analysis of the active site of porcine pancreatic elastase. The inhibition constants for the inhibitors are used in combination with the crystal structures to understand the specificity of the different elastase subsites.