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Ligands
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ACN Acetone
Non-standard Residues
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CSO S-hydroxycysteine
Glycosylation
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Code : 1GNS   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : SUBTILISIN BPN'
Release Data : 2002-06-27
Compound :
mol_id molecule chains
1 SUBTILISIN BPN' A
ec: 3.4.21.62
fragment: RESIDUES 111-181,191-382
mutation: YES
Source :
mol_id organism_scientific expression_system
1 BACILLUS AMYLOLIQUEFACIENS  (taxid:1390) ESCHERICHIA COLI  (taxid:469008)
expression_system_strain: BL21(DE3)
Authors : Almog, O., Gallagher, D.T., Ladner, J.E., Strausberg, S., Alexander, P.
Keywords : HYDROLASE, SERINE PROTEINASE
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Structural Basis of Thermostability. Analysis of Stabilizing Mutations in Subtilisin Bpn'.

Almog, O.,Gallagher, D.T.,Ladner, J.E.  et al.
(2002)  J.Biol.Chem.  277 : 27553

PubMed: 12011071
DOI: 10.1074/JBC.M111777200

Chain : A
UniProt : P00782 (SUBT_BACAM)
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 -
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