P01062IBB_VIGRRBowman-Birk type trypsin inhibitorVigna radiata var. radiataMung beanPhaseolus aureusEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeVignaComplete amino acid sequence of mung bean trypsin inhibitor.PROTEIN SEQUENCEThe 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin.X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS)DISULFIDE BONDSStudies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin.X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 10-31SEQUENCE REVISIONDISULFIDE BONDSFunctionally this inhibitor is unusual in that it stoichiometrically inhibits trypsin in a molar ratio of 1:2.The specificities and functions of this superfamily of inhibitors depend not only on the active sites within the domains, but also upon the amino acid composition, and resulting molecular conformation, surrounding these regions.Three isoinhibitors are also found whose amino ends differ slightly from that shown.Belongs to the Bowman-Birk serine protease inhibitor family.3D-structureDirect protein sequencingDisulfide bondProtease inhibitorReference proteomeSerine protease inhibitorHDDKSHDEPSESSEPCCDSCDCTKSIPPECHCANIRLNSCHSACKSCICTRSMPGKCRCLDTDDFCYKPCESMDKD
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