4U30

Human mesotrypsin complexed with bikunin Kunitz domain 2

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
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	d4u30a_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d4u30b_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d4u30c_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d4u30d_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E [auth X]	d4u30x_	Small proteins	BPTI-like	BPTI-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F [auth Y]	d4u30y_	Small proteins	BPTI-like	BPTI-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G [auth Z]	d4u30z_	Small proteins	BPTI-like	BPTI-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H [auth W]	d4u30w_	Small proteins	BPTI-like	BPTI-like	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	SCOP2B Superfamily	Trypsin-like serine proteases	8036274	3000114	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Trypsin-like serine proteases	8036274	3000114	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Trypsin-like serine proteases	8036274	3000114	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Trypsin-like serine proteases	8036274	3000114	SCOP2B (2022-06-29)
E [auth X]	SCOP2B Superfamily	BPTI-like	8038548	3000628	SCOP2B (2022-06-29)
F [auth Y]	SCOP2B Superfamily	BPTI-like	8038548	3000628	SCOP2B (2022-06-29)
G [auth Z]	SCOP2B Superfamily	BPTI-like	8038548	3000628	SCOP2B (2022-06-29)
H [auth W]	SCOP2B Superfamily	BPTI-like	8038548	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	Trypsin_1	e4u30A1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B	Trypsin_1	e4u30B1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
C	Trypsin_1	e4u30C1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
D	Trypsin_1	e4u30D1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
E [auth X]	Kunitz_BPTI	e4u30X1	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 [auth Y]	Kunitz_BPTI	e4u30Y1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
G [auth Z]	Kunitz_BPTI	e4u30Z1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
H [auth W]	Kunitz_BPTI	e4u30W1	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	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
C	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
D	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
E [auth X]	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
F [auth Y]	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
G [auth Z]	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
H [auth W]	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	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
E [auth X], F [auth Y], G [auth Z], H [auth W]	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	Trypsin-3	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding 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	humoral immune response biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response immune response defense response to symbiont response to external stimulus antimicrobial humoral response response to biotic stimulus defense response to other organism response to stress immune system process response to external biotic stimulus humoral immune response biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response immune response defense response to symbiont response to external stimulus antimicrobial humoral response response to biotic stimulus defense response to other organism response to stress immune system process response to external biotic stimulus epithelium migration multicellular organismal process tissue migration endothelial cell migration ameboidal-type cell migration epithelial cell migration cell migration cellular process cell motility organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process zymogen activation cellular biosynthetic process cellular metabolic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process organic substance biosynthetic process protein processing digestion	membrane-bounded organelle intracellular anatomical structure tertiary granule lumen membrane-enclosed lumen intracellular vesicle cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen tertiary granule intracellular organelle organelle lumen cytoplasmic vesicle organelle membrane-bounded organelle intracellular anatomical structure tertiary granule lumen membrane-enclosed lumen intracellular vesicle cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen tertiary granule intracellular organelle organelle lumen cytoplasmic vesicle organelle secretory granule secretory vesicle cytoplasm vesicle extracellular region extracellular space
E [auth X], F [auth Y], G [auth Z], H [auth W]	Trypstatin	oxidoreductase activity catalytic activity binding carbohydrate binding 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 identical protein binding oxidoreductase activity catalytic activity binding carbohydrate binding 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 identical protein binding protein binding protein homodimerization activity protein dimerization activity organic cyclic compound binding tetrapyrrole binding heme binding channel regulator activity transporter inhibitor activity calcium channel inhibitor activity ion channel inhibitor activity ion channel regulator activity calcium channel regulator activity transporter regulator activity channel inhibitor activity organic acid binding ion binding anion binding calcium oxalate binding carboxylic acid binding small molecule binding protein-containing complex binding immunoglobulin binding IgA binding	multi-multicellular organism process multicellular organismal process reproductive process female pregnancy multi-organism reproductive process regulation of biological process response to stimulus immune response negative regulation of response to stimulus negative regulation of immune response biological regulation negative regulation of biological process regulation of response to stimulus negative regulation of immune system process multi-multicellular organism process multicellular organismal process reproductive process female pregnancy multi-organism reproductive process regulation of biological process response to stimulus immune response negative regulation of response to stimulus negative regulation of immune response biological regulation negative regulation of biological process regulation of response to stimulus negative regulation of immune system process immune system process regulation of immune response regulation of immune system process cellular response to stimulus regulation of cellular process signaling negative regulation of signaling negative regulation of intracellular signal transduction regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication negative regulation of JNK cascade regulation of intracellular signal transduction JNK cascade intracellular signaling cassette negative regulation of cellular process signal transduction regulation of signaling regulation of JNK cascade regulation of MAPK cascade negative regulation of signal transduction MAPK cascade regulation of cell communication cellular process negative regulation of MAPK cascade organonitrogen compound catabolic process pigment catabolic process pigment metabolic process heme metabolic process organonitrogen compound metabolic process catabolic process tetrapyrrole metabolic process organic cyclic compound catabolic process organic cyclic compound metabolic process organic substance metabolic process heme catabolic process porphyrin-containing compound catabolic process metabolic process porphyrin-containing compound metabolic process organic substance catabolic process tetrapyrrole catabolic process cell adhesion	membrane-bounded organelle mitochondrial membrane intracellular anatomical structure organelle inner membrane mitochondrion membrane cellular anatomical entity intracellular membrane-bounded organelle mitochondrial inner membrane intracellular organelle organelle envelope mitochondrial envelope organelle cytoplasm membrane-bounded organelle mitochondrial membrane intracellular anatomical structure organelle inner membrane mitochondrion membrane cellular anatomical entity intracellular membrane-bounded organelle mitochondrial inner membrane intracellular organelle organelle envelope mitochondrial envelope organelle cytoplasm organelle membrane nuclear membrane nucleus endomembrane system nuclear envelope extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix cell surface cytosol plasma membrane blood microparticle endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A, B, C, D	IPR001314	Peptidase S1A, chymotrypsin family	Family
A, B, C, D	IPR001254	Serine proteases, trypsin domain	Domain
A, B, C, D	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A, B, C, D	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR002968	Alpha-1-microglobulin	Family
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR002223	Pancreatic trypsin inhibitor Kunitz domain	Domain
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR012674	Calycin	Homologous Superfamily
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR029856	Protein AMBP	Family
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR000566	Lipocalin/cytosolic fatty-acid binding domain	Domain
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR022272	Lipocalin family conserved site	Conserved Site
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR020901	Proteinase inhibitor I2, Kunitz, conserved site	Conserved Site
E [auth X], F [auth Y], G [auth Z], H [auth W]	IPR036880	Pancreatic trypsin inhibitor Kunitz domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P35030	urinary bladder cancer primitive neuroectodermal tumor astrocytic tumor diabetes mellitus large cell medulloblastoma malignant mesothelioma oligodendroglioma pancreatic intraductal papillary-mucinous neoplasm Prevention of deep vein thrombosis psoriasis urinary bladder neoplasm atypical teratoid rhabdoid tumor glioblastoma malignant ependymoma malignant pancreatic neoplasm urinary bladder cancer primitive neuroectodermal tumor astrocytic tumor diabetes mellitus large cell medulloblastoma malignant mesothelioma oligodendroglioma pancreatic intraductal papillary-mucinous neoplasm Prevention of deep vein thrombosis psoriasis urinary bladder neoplasm atypical teratoid rhabdoid tumor glioblastoma malignant ependymoma malignant pancreatic neoplasm pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia subependymal giant cell astrocytoma cystic fibrosis Hashimoto thyroiditis malignant glioma medulloblastoma pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma
E [auth X], F [auth Y], G [auth Z], H [auth W]	Pharos: P02760	transitional cell carcinoma Neoplasm Invasiveness acute kidney failure drug-induced liver injury pancreatic intraductal papillary-mucinous neoplasm hereditary coproporphyria osteoarthritis pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia pancreatic intraductal papillary-mucinous carcinoma

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.