Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTrypsin-like serine proteases 8042128 3000114 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyTrypsin-like serine proteases 8042128 3000114 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyBPTI-like 8038485 3000628 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyBPTI-like 8038485 3000628 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATrypsin_1e1p2nA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrel 2F: Trypsin_1ECOD (1.6)
CTrypsin_1e1p2nC1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrel 2F: Trypsin_1ECOD (1.6)
BKunitz_BPTIe1p2nB1 A: few secondary structure elementsX: BPTI-like (From Topology)H: BPTI-like (From Topology)T: BPTI-likeF: Kunitz_BPTIECOD (1.6)
DKunitz_BPTIe1p2nD1 A: few secondary structure elementsX: BPTI-like (From Topology)H: BPTI-like (From Topology)T: BPTI-likeF: Kunitz_BPTIECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, C
PF00089Trypsin (Trypsin)Trypsin- Domain
B, D
PF00014Kunitz/Bovine pancreatic trypsin inhibitor domain (Kunitz_BPTI)Kunitz/Bovine pancreatic trypsin inhibitor domainIndicative 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

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, C
Chymotrypsinogen A
B, D
Pancreatic trypsin inhibitor