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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
CLB D-para-chlorophenyl-1-acetamidoboronic acid alanine
Glycosylation
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Modification
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Code : 1VSB   PDBj   RCSB PDB   PDBe
Header : SERINE PROTEASE
Title : SUBTILISIN CARLSBERG L-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
Release Data : 1998-03-18
Compound :
mol_id molecule chains synonym
1 SUBTILISIN CARLSBERG, TYPE VIII A SUBTILOPEPTIDASE A
ec: 3.4.21.62
Source :
mol_id organism_scientific
1 Bacillus licheniformis  (taxid:1402)
other_details: PURCHASED FROM SIGMA
Authors : Stoll, V.S., Eger, B.T., Hynes, R.C., Martichonok, V., Jones, J.B., Pai, E.F.
Keywords : SERINE PROTEASE, HYDROLASE, BORONIC ACID INHIBITORS
Exp. method : X-RAY DIFFRACTION ( 2.1 Å )
Citation :

Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.

Stoll, V.S.,Eger, B.T.,Hynes, R.C.  et al.
(1998)  Biochemistry  37 : 451 - 462

PubMed: 9425066
DOI: 10.1021/bi971166o

Probing the Specificity of the Serine Proteases Subtilisin Carlsberg and A-Chymotrypsin with Enantiomeric 1-Acetamido Boronic Acids. An Unexpected Reversal of the Normal "L"-Stereoselectivity Preference

Martichonok, V.,Jones, J.B.
(1996)  J.Am.Chem.Soc.  118 : 950

Probing the Specificity of the S1 Binding Site of Subtilisin Carlsberg with Boronic Acids

Seufer-Wasserthal, P.,Martichonok, V.,Keller, T.H.  et al.
(1994)  Bioorg.Med.Chem.  2 : 35

Enzyme Crystal Structure in a Neat Organic Solvent

Fitzpatrick, P.A.,Steinmetz, A.C.,Ringe, D.  et al.
(1993)  Proc.Natl.Acad.Sci.USA  90 : 8653

The Structure of Subtilopeptidase A. I. X-Ray Crystallographic Data

Petsko, G.A.,Tsernoglou, D.
(1976)  J.Mol.Biol.  106 : 453

Chain : A
UniProt : P00780 (SUBC_BACLI)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. 3.4.21.62 PubMed:11109488, Ref.4
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