Structure for peptidase S08.001: subtilisin Carlsberg

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

PDB	Organism	Resolution	Comment
1SCN	Bacillus licheniformis	1.90 Å	complex with N-tert-butoxycarbonyl-Ala-Pro-Phe-O-benzoyl hydroxylamine
Catalytic residues are shown in ball-and-stick representation: Asp137 in pink, His168 in purple and Ser325 in orange. N-tert-butoxycarbonyl-Ala-Pro-Phe-O-benzoyl hydroxylamine is shown in grey in ball-and-stick representation.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Bacillus licheniformis
complex with barley chymotrypsin inhibitor CI-2A(M59P): OBSOLETE ENTRY	1.80 Å	1A10	1A10	1A10	1A10	1A10	1A10
complex with chymotrypsin inhibitor CI-2A: OBSOLETE ENTRY	1.05 Å	1A1Y	1A1Y	1A1Y	1A1Y	1A1Y	1A1Y
mature peptidase	2.60 Å	1AF4	1AF4	1AF4	1AF4	1AF4	1AF4	Schmitke et al., 1997
complex with L-naphthyl-1-acetamido boronic acid inhibitor	2.60 Å	1AV7	1AV7	1AV7	1AV7	1AV7	1AV7	Stoll et al., 1998
complex with D-para-chlorophenyl-1-acetamido boronic acid inhibitor	2.00 Å	1AVT	1AVT	1AVT	1AVT	1AVT	1AVT	Stoll et al., 1998
trans-cinnamoyl-subtilisin in andhydrous acetonitrile	2.15 Å	1BE6	1BE6	1BE6	1BE6	1BE6	1BE6	Schmitke et al., 1998
trans-cinnamoyl-subtilisin in water	2.20 Å	1BE8	1BE8	1BE8	1BE8	1BE8	1BE8	Schmitke et al., 1998
in 40% acetonitrile	2.30 Å	1BFK	1BFK	1BFK	1BFK	1BFK	1BFK	Schmitke et al., 1998
in 20% dioxane	2.20 Å	1BFU	1BFU	1BFU	1BFU	1BFU	1BFU	Schmitke et al., 1998
under xenon pressure	2.16 Å	1C3L	1C3L	1C3L	1C3L	1C3L	1C3L	Prange et al., 1998
NMR structure; complex with barley chymotrypsin inhibitor-2	0.00 Å	1CIS	1CIS	1CIS	1CIS	1CIS	1CIS	Osmark et al., 1993
complex with eglin C	1.20 Å	1CSE	1CSE	1CSE	1CSE	1CSE	1CSE	Bode et al., 1987
complex with tomato inhibitor-II	2.50 Å	1OYV	1OYV	1OYV	1OYV	1OYV	1OYV	Barrette-Ng et al., 2003
complex with inhibitor turkey ovomucoid third domain	1.10 Å	1R0R	1R0R	1R0R	1R0R	1R0R	1R0R	Horn et al., 2003
mature peptidase	2.50 Å	1SBC	1SBC	1SBC	1SBC	1SBC	1SBC	Neidhart & Petsko, 1988
mature peptidase	2.00 Å	1SCA	1SCA	1SCA	1SCA	1SCA	1SCA	Fitzpatrick et al., 1993
acetonitrile soaked crystals	2.30 Å	1SCB	1SCB	1SCB	1SCB	1SCB	1SCB	Fitzpatrick et al., 1993
mature peptidase	2.30 Å	1SCD	1SCD	1SCD	1SCD	1SCD	1SCD	Fitzpatrick et al., 1994
complex with N-tert-butoxycarbonyl-Ala-Pro-Phe-O-benzoyl hydroxylamine	1.90 Å	1SCN	1SCN	1SCN	1SCN	1SCN	1SCN	Steinmetz et al., 1994
complex with L-para-chlorophenyl-1-acetamido boronic acid inhibitor	2.10 Å	1VSB	1VSB	1VSB	1VSB	1VSB	1VSB	Stoll et al., 1998
complex with turkey ovomucoid third domain	1.55 Å	1YU6	1YU6	1YU6	1YU6	1YU6	1YU6	Maynes et al., 2005
complex with N-acetyl eglin C	1.80 Å	2SEC	2SEC	2SEC	2SEC	2SEC	2SEC	McPhalen & James, 1988
crystallographic analysis of counter-ion effects in acetonitrile	2.24 Å	2WUV	2WUV	2WUV	2WUV	2WUV	2WUV
crystallographic analysis of counter-ion effects in acetonitrile (native data)	2.23 Å	2WUW	2WUW	2WUW	2WUW	2WUW	2WUW
complex with horseshoe crab Kazal-type serine protease inhibitor	2.60 Å	3QTL	3QTL	3QTL	3QTL	3QTL	3QTL	Shenoy et al., 2011
bond length analysis of Asp, Glu and His residues	1.26 Å	3UNX	3UNX	3UNX	3UNX	3UNX	3UNX
complex with D-naphthyl-1-acetamido boronic acid inhibitor	2.60 Å	3VSB	3VSB	3VSB	3VSB	3VSB	3VSB	Stoll et al., 1998
extensive counter-ion interactions in aqueous medium, cs derivative	2.29 Å	4C3U	4C3U	4C3U	4C3U	4C3U	4C3U
extensive counter-ion interactions in aqueous medium, no cs soak	2.26 Å	4C3V	4C3V	4C3V	4C3V	4C3V	4C3V
complex with Streptomyces caespitosus sermetstatin	2.25 Å	4HX2	4HX2	4HX2	4HX2	4HX2	4HX2
subtilisin serine protease modified with the protease inhibitor cyanobenzylsulfonylfluoride	1.27 Å	6DWQ	6DWQ	6DWQ	6DWQ	6DWQ	6DWQ