1S01 | pdb_00001s01

LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1s01a_	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Subtilisin	Bacillus velezensis (Bacillus amyloliquefaciens ) [TaxId: 1390 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Subtilisin-like	8042613	3000226	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_S8	e1s01A1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00082	Subtilase family (Peptidase_S8)	Subtilase family	Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7 ...	Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Subtilisin BPN'	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity cation binding ion binding binding metal ion binding small molecule binding	sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation multicellular organismal process regulation of body fluid levels response to stimulus regulation of response to external stimulus negative regulation of biological process regulation of response to wounding regulation of coagulation response to stress sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation multicellular organismal process regulation of body fluid levels response to stimulus regulation of response to external stimulus negative regulation of biological process regulation of response to wounding regulation of coagulation response to stress regulation of response to stress coagulation regulation of multicellular organismal process regulation of biological quality response to wounding regulation of hemostasis wound healing regulation of biological process negative regulation of response to stimulus negative regulation of wound healing regulation of blood coagulation negative regulation of blood coagulation biological regulation hemostasis response to external stimulus negative regulation of response to wounding blood coagulation negative regulation of hemostasis fibrinolysis negative regulation of coagulation regulation of response to stimulus negative regulation of response to external stimulus regulation of wound healing negative regulation of multicellular organismal process proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR023828	Peptidase S8, subtilisin, Ser-active site	Active Site
A	IPR022398	Peptidase S8, subtilisin, His-active site	Active Site
A	IPR000209	Peptidase S8/S53 domain	Domain
A	IPR054399	Fervidolysin-like, N-terminal prodomain	Domain
A	IPR015500	Peptidase S8, subtilisin-related	Family
A	IPR036852	Peptidase S8/S53 domain superfamily	Homologous Superfamily
A	IPR023827	Peptidase S8, subtilisin, Asp-active site	Active Site
A	IPR050131	Subtilisin-like serine protease	Family
A	IPR037045	Peptidase S8 propeptide/proteinase inhibitor I9 superfamily	Homologous Superfamily
A	IPR034202	Subtilisin Carlsberg-like catalytic domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	SCH	Parent Component: CYS RESID: AA0101 PSI-MOD : L-cysteine methyl disulfide MOD:00110

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	subtilisin M-CSA #723	Subtilisin is an extracellular enzyme secreted by Bacillus amyloliquefaciens and belongs to the alpha/beta subtilase family. It is a serine-class endoprotease, hydrolysing peptide bonds with broad specificity and a preference for a large uncharged residue in the P1 binding site.	Defined by 4 residues: ASP:A-32HIS:A-64ASN:A-155SER:A-221 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.21.62 (PDB Primary Data) Search M-CSA Motif + EC 3.4.21.62

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.