1Y62 | pdb_00001y62

A 2.4 crystal structure of conkunitzin-S1, a novel Kunitz-fold cone snail neurotoxin.

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Small Kunitz-type inhibitors & BPTI-like toxins	8070130	4003337	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	BPTI-like	8070131	3000628	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	BPTI-like	8070131	3000628	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	BPTI-like	8070131	3000628	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	BPTI-like	8070131	3000628	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	BPTI-like	8070131	3000628	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	BPTI-like	8070131	3000628	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	Kunitz_BPTI	e1y62A1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
B	Kunitz_BPTI	e1y62B1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
C	Kunitz_BPTI	e1y62C1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
D	Kunitz_BPTI	e1y62D1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
E	Kunitz_BPTI	e1y62E1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
F	Kunitz_BPTI	e1y62F1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
B	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
C	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
D	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
E	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
F	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00014	Kunitz/Bovine pancreatic trypsin inhibitor domain (Kunitz_BPTI)	Kunitz/Bovine pancreatic trypsin inhibitor domain	Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the ...	Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP, Swiss:P17726). This is a highly selective inhibitor of factor Xa in the blood coagulation pathways [1]. TAP molecules are highly dipolar [2], and are arranged to form a twisted two- stranded antiparallel beta-sheet followed by an alpha helix [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Conkunitzin-S1	enzyme regulator activity peptidase activity peptidase regulator activity catalytic activity, acting on a protein serine hydrolase activity serine-type endopeptidase inhibitor activity hydrolase activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity molecular function inhibitor activity molecular function regulator activity serine-type peptidase activity serine-type endopeptidase activity enzyme regulator activity peptidase activity peptidase regulator activity catalytic activity, acting on a protein serine hydrolase activity serine-type endopeptidase inhibitor activity hydrolase activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity molecular function inhibitor activity molecular function regulator activity serine-type peptidase activity serine-type endopeptidase activity catalytic activity endopeptidase activity monoatomic cation transmembrane transporter activity channel regulator activity ion channel regulator activity monoatomic ion channel activity potassium ion transmembrane transporter activity potassium channel activity potassium channel regulator activity monoatomic cation channel activity passive transmembrane transporter activity inorganic molecular entity transmembrane transporter activity channel activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity transporter regulator activity metal ion transmembrane transporter activity transmembrane transporter activity toxin activity	-	cellular anatomical structure extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR002223	Pancreatic trypsin inhibitor Kunitz domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR050098	Tissue factor pathway inhibitor/Kunitz-type serine protease inhibitor-like	Family
A, B, C, D, E A, B, C, D, E, F	IPR036880	Pancreatic trypsin inhibitor Kunitz domain superfamily	Homologous Superfamily

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.