1F34 | pdb_00001f34

CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1f34b_	Alpha and beta proteins (a+b)	Pepsin inhibitor-3	Pepsin inhibitor-3	Pepsin inhibitor-3	Pepsin inhibitor-3	pig roundworm (Ascaris suum ) [TaxId: 6253 ],	SCOPe (2.08)
A	d1f34a_	All beta proteins	Acid proteases	Acid proteases	Pepsin-like	Pepsin(ogen)	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Pepsin inhibitor-3	8035718	3001417	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Acid proteases	8042474	3001059	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)
B	Pepsin-I3	e1f34B1	A: a+b duplicates or obligate multimers	X: Pepsin inhibitor-3 (From Topology)	H: Pepsin inhibitor-3 (From Topology)	T: Pepsin inhibitor-3	F: Pepsin-I3	ECOD (1.6)
A	Asp_C	e1f34A2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
A	Asp_N	e1f34A3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.1120.50	Alpha Beta	2-Layer Sandwich	Arylsulfatase, C-terminal domain	Pepsin inhibitor-3	CATH (4.3.0)
A	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B	PF06394	Pepsin inhibitor-3-like repeated domain (Pepsin-I3)	Pepsin inhibitor-3-like repeated domain	Pepsin inhibitor-3 consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the active site flap region of pepsin ...	Pepsin inhibitor-3 consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the active site flap region of pepsin [1]. The two domains are tandem repeats of sequence, and has therefore been termed repeated domain.	Domain
A	PF00026	Eukaryotic aspartyl protease (Asp)	Eukaryotic aspartyl protease	Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (Pfam:PF00077), which are much smaller a ...	Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (Pfam:PF00077), which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B	MAJOR PEPSIN INHIBITOR PI-3	enzyme regulator activity molecular function inhibitor activity peptidase regulator activity molecular function regulator activity enzyme inhibitor activity aspartic-type endopeptidase inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity	-	cellular anatomical structure extracellular region
A	PEPSIN A	aspartic-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity aspartic-type endopeptidase activity catalytic activity endopeptidase activity	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B	IPR010480	Pepsin inhibitor-3-like repeated domain	Domain
B	IPR051901	Protease Inhibitor I33	Family
B	IPR038412	Pepsin inhibitor-3 domain superfamily	Homologous Superfamily
A	IPR001461	Aspartic peptidase A1	Family
A	IPR012848	Aspartic peptidase, N-terminal	Domain
A	IPR034162	Pepsin catalytic domain	Domain
A	IPR033121	Peptidase family A1 domain	Domain
A	IPR021109	Aspartic peptidase domain superfamily	Homologous Superfamily
A	IPR001969	Aspartic peptidase, active site	Active Site

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	SEP	Parent Component: SER RESID: AA0037 PSI-MOD : O-phospho-L-serine MOD:00046

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.