Brand  (β version)

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain:

Ligands
Code Name Link
ACN Acetone
CA Calcium ion
Modified Residues
Code Name Link
MIS Monoisopropylphosphorylserine
Code : 1A2Q   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : SUBTILISIN BPN' MUTANT 7186
Release Data : 1998-04-29
Compound :
mol_id molecule chains
1 SUBTILISIN BPN' A
ec: 3.4.21.62
mutation: T22C, S87C, G169A, N218S
Source :
mol_id organism_scientific expression_system
1 Bacillus amyloliquefaciens  (taxid:1390) Bacillus subtilis  (taxid:1423)
strain: GX7186
cellular_location: SECRETED
expression_system_strain: GX7186
expression_system_cellular_location: SECRETED
expression_system_plasmid: PGX7186
Authors : Gilliland, G.L., Whitlow, M., Howard, A.J.
Keywords : HYDROLASE, SERINE PROTEASE, SPORULATION
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.

Pantoliano, M.W.,Whitlow, M.,Wood, J.F.  et al.
(1989)  Biochemistry  28 : 7205 - 7213

PubMed: 2684274
DOI: 10.1021/bi00444a012

Protein Engineering of Subtilisin Bpn': Enhanced Stabilization Through the Introduction of Two Cysteines to Form a Disulfide Bond

Pantoliano, M.W.,Ladner, R.C.,Bryan, P.N.  et al.
(1987)  Biochemistry  26 : 2077

Proteases of Enhanced Stability: Characterization of a Thermostable Variant of Subtilisin

Bryan, P.N.,Rollence, M.L.,Pantoliano, M.W.  et al.
(1986)  Proteins  1 : 326

Atomic Coordinates for Subtilisin Bpn' (or Novo)

Alden, R.A.,Birktoft, J.J.,Kraut, J.  et al.
(1971)  Biochem.Biophys.Res.Commun.  45 : 337

Chain : A
UniProt : P00782 (SUBT_BACAM)
Reaction : Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.