Entry Database : PDB / ID : 4o9v Structure visualization Downloads & linksTitle Crystal structure of matriptase in complex with inhibitor ComponentsPeptide CGLR Suppressor of tumorigenicity 14 protein DetailsKeywords HYDROLASE/HYDROLASE INHIBITOR / MATRIPTASE / Trypsin-like serine proteinase fold / Protease / Small molecule inhibitor / HYDROLASE-HYDROLASE INHIBITOR complexFunction / homology Function and homology informationFunction Domain/homology Component
matriptase / epithelial cell morphogenesis involved in placental branching / acrosome reaction / Formation of the cornified envelope / keratinocyte differentiation / serine-type peptidase activity / neural tube closure / protein catabolic process / basolateral plasma membrane / external side of plasma membrane ... matriptase / epithelial cell morphogenesis involved in placental branching / acrosome reaction / Formation of the cornified envelope / keratinocyte differentiation / serine-type peptidase activity / neural tube closure / protein catabolic process / basolateral plasma membrane / external side of plasma membrane / serine-type endopeptidase activity / proteolysis / extracellular space / plasma membrane Similarity search - Function Peptidase S1A, matripase / SEA domain superfamily / SEA domain profile. / SEA domain / SEA domain / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Spermadhesin, CUB domain superfamily ... Peptidase S1A, matripase / SEA domain superfamily / SEA domain profile. / SEA domain / SEA domain / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Spermadhesin, CUB domain superfamily / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution : 1.9 Å DetailsAuthors Rao, K.N. / Chandra, B.R. / Ashok, K.N. / Chakshusmathi, G. / Ramesh, K.S. / Subramanya, H.S. CitationJournal : Bioorg.Med.Chem. / Year : 2014Title : Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy.Authors: Goswami, R. / Mukherjee, S. / Ghadiyaram, C. / Wohlfahrt, G. / Sistla, R.K. / Nagaraj, J. / Satyam, L.K. / Subbarao, K. / Palakurthy, R.K. / Gopinath, S. / Krishnamurthy, N.R. / Ikonen, T. / ... Authors : Goswami, R. / Mukherjee, S. / Ghadiyaram, C. / Wohlfahrt, G. / Sistla, R.K. / Nagaraj, J. / Satyam, L.K. / Subbarao, K. / Palakurthy, R.K. / Gopinath, S. / Krishnamurthy, N.R. / Ikonen, T. / Moilanen, A. / Subramanya, H.S. / Kallio, P. / Ramachandra, M. History Deposition Jan 3, 2014 Deposition site : RCSB / Processing site : PDBJRevision 1.0 May 28, 2014 Provider : repository / Type : Initial releaseRevision 1.1 Nov 8, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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