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
CL Chloride ion
Non-standard Residues
Code Name Show
HPH (2s)-2-amino-3-phenylpropane-1,1-diol
Glycosylation
Code Name Emphasize
Modification
Code Name Show
PHQ Benzyl chlorocarbonate
0QE Chloromethane
Code : 1DLK   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR
Release Data : 2000-05-03
Compound :
mol_id molecule chains
1 Thrombin light chain A,C
ec: 3.4.21.1
fragment: RESIDUES 1-13
mol_id molecule chains
2 Thrombin heavy chain B,D
ec: 3.4.21.1
fragment: RESIDUES 16-245
mol_id molecule chains
3 peptidic inhibitor E,F
Source :
mol_id organism_scientific organism_common
1 Bos taurus  (taxid:9913) Cattle
organ: PANCREAS
mol_id organism_scientific organism_common
2 Bos taurus  (taxid:9913) Cattle
organ: PANCREAS
mol_id organism_scientific
3
synthetic: yes
other_details: this sequence was synthetically constructed
Authors : Mac Sweeney, A., Birrane, G., Walsh, M.A., O'Connell, T., Malthouse, J.P.G.
Keywords : Delta-chymotrypsin, peptidic inhibior, chloromethyl ketone, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.14 Å )
Citation :

Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.

Mac Sweeney, A.,Birrane, G.,Walsh, M.A.  et al.
(2000)  Acta Crystallogr.,Sect.D  56 : 280 - 286

PubMed: 10713514
DOI: 10.1107/S0907444999016583

Chain : B, D
UniProt : P00766 (CTRA_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|- Xaa. 3.4.21.1 PROSITE-ProRule:PRU10078, PROSITE-ProRule:PRU10079
-