7JQV

Crystal structure of the R64F mutant of Bauhinia Bauhinioides Kallikrein Inhibitor complexed with Human Kallikrein 4

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth E]	d7jqve_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth E]	SCOP2B Superfamily	Trypsin-like serine proteases	8103731	3000114	SCOP2B (2022-06-29)
B [auth I]	SCOP2B Superfamily	STI-like	8070249	3000715	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 [auth E]	Trypsin_1	e7jqvE1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B [auth I]	Kunitz_legume	e7jqvI1	A: beta duplicates or obligate multimers	X: beta-Trefoil (From Topology)	H: beta-Trefoil (From Topology)	T: beta-Trefoil	F: Kunitz_legume	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth E]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
B [auth I]	PF00197	Trypsin and protease inhibitor (Kunitz_legume)	Trypsin and protease inhibitor	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth E]	Kallikrein 4 (Prostase, enamel matrix, prostate), isoform CRA_a	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	developmental process anatomical structure morphogenesis odontogenesis of dentin-containing tooth anatomical structure formation involved in morphogenesis anatomical structure development odontogenesis animal organ development amelogenesis animal organ morphogenesis biomineral tissue development tissue development cellular component organization cellular component disassembly extracellular matrix disassembly developmental process anatomical structure morphogenesis odontogenesis of dentin-containing tooth anatomical structure formation involved in morphogenesis anatomical structure development odontogenesis animal organ development amelogenesis animal organ morphogenesis biomineral tissue development tissue development cellular component organization cellular component disassembly extracellular matrix disassembly extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure extracellular region membrane-bounded organelle intracellular anatomical structure intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cytoplasmic vesicle organelle secretory granule secretory vesicle cytoplasm vesicle
B [auth I]	Kunitz-type inihibitor	enzyme regulator activity molecular function inhibitor activity peptidase regulator activity serine-type endopeptidase inhibitor activity molecular function regulator activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity	negative regulation of hydrolase activity negative regulation of proteolysis regulation of cellular process regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity regulation of primary metabolic process negative regulation of peptidase activity regulation of proteolysis proteolysis negative regulation of cellular process protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process negative regulation of hydrolase activity negative regulation of proteolysis regulation of cellular process regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity regulation of primary metabolic process negative regulation of peptidase activity regulation of proteolysis proteolysis negative regulation of cellular process protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biological process regulation of protein metabolic process negative regulation of metabolic process biological regulation negative regulation of molecular function regulation of peptidase activity primary metabolic process regulation of macromolecule metabolic process regulation of molecular function regulation of hydrolase activity metabolic process cellular process macromolecule metabolic process regulation of metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A [auth E]	IPR001314	Peptidase S1A, chymotrypsin family	Family
A [auth E]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
A [auth E]	IPR001254	Serine proteases, trypsin domain	Domain
A [auth E]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A [auth E]	IPR050127	Serine Proteases (Peptidase S1 Family)	Family
A [auth E]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
B [auth I]	IPR002160	Proteinase inhibitor I3, Kunitz legume	Family
B [auth I]	IPR011065	Kunitz inhibitor STI-like superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth E]	Pharos: Q9Y5K2	amelogenesis imperfecta amelogenesis imperfecta type 2A1 large cell medulloblastoma ovarian cancer Amelogenesis Imperfecta hypomaturation type angioedema medulloblastoma prostate carcinoma hypertensive disorder osteosarcoma

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.