Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
CA Calcium ion
DOD Deuterated water
FRW 4-[[(2s)-3-methyl-1-oxo-1-[(2s)-2-[[(3s)-1,1,1-trifluoro-4-methyl-2-oxo-pentan-3-yl]carbamoyl]pyrrolidin-1-yl]butan-2-yl]carbamoyl]benzoic acid
SO4 Sulfate ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3HGN   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Structure of porcine pancreatic elastase complexed with a potent peptidyl inhibitor FR130180 determined by neutron crystallography
Release Data : 2009-07-28
Compound :
mol_id molecule chains
1 Elastase-1 A
ec: 3.4.21.36
Source :
mol_id organism_scientific organism_common
1 Sus scrofa  (taxid:9823) Pig
other_details: Porcine Pancreatic
Authors : Tamada, T., Kinoshita, T., Kuroki, R., Tada, T.
Keywords : Chymotrypsin Family, Hydrolase, Serine Protease, Disulfide bond, Metal-binding, Protease, Secreted, Zymogen
Exp. method : NEUTRON DIFFRACTION ( 1.650 Å )
Citation :

Combined High-Resolution Neutron and X-ray Analysis of Inhibited Elastase Confirms the Active-Site Oxyanion Hole but Rules against a Low-Barrier Hydrogen Bond

Tamada, T.,Kinoshita, T.,Kurihara, K.  et al.
(2009)  J.Am.Chem.Soc.  131 : 11033 - 11040

PubMed: 19603802
DOI: 10.1021/ja9028846

Crystallization of porcine pancreatic elastase and a preliminary neutron diffraction experiment

Kinoshita, T.,Tamada, T.,Imai, K.  et al.
(2007)  Acta Crystallogr.,Sect.F  63 : 315 - 317

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