Entry Database : PDB / ID : 4u32 Structure visualization Downloads & linksTitle Human mesotrypsin complexed with HAI-2 Kunitz domain 1 ComponentsKunitz-type protease inhibitor 2 Trypsin-3 DetailsKeywords HYDROLASE/HYDROLASE INHIBITOR / serine protease / protease inhibitor / protein-protein interaction / protein degradation / proteolysis / substrate specificity / enzyme kinetics / HYDROLASE-HYDROLASE INHIBITOR complexFunction / homology Function and homology informationFunction Domain/homology Component
Signaling by MST1 / epithelial cell morphogenesis involved in placental branching / Uptake of dietary cobalamins into enterocytes / negative regulation of neural precursor cell proliferation / basement membrane organization / MET Receptor Activation / negative regulation of cell motility / cellular response to BMP stimulus / antimicrobial humoral response / Alpha-defensins ... Signaling by MST1 / epithelial cell morphogenesis involved in placental branching / Uptake of dietary cobalamins into enterocytes / negative regulation of neural precursor cell proliferation / basement membrane organization / MET Receptor Activation / negative regulation of cell motility / cellular response to BMP stimulus / antimicrobial humoral response / Alpha-defensins / zymogen activation / Antimicrobial peptides / establishment or maintenance of cell polarity / endopeptidase inhibitor activity / negative regulation of cell-cell adhesion / endothelial cell migration / trypsin / digestion / serine-type peptidase activity / neural tube closure / serine-type endopeptidase inhibitor activity / tertiary granule lumen / membrane => GO:0016020 / serine-type endopeptidase activity / calcium ion binding / Neutrophil degranulation / proteolysis / extracellular space / extracellular region / plasma membrane / cytoplasm Similarity search - Function Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / Few Secondary Structures ... Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / Few Secondary Structures / Irregular / Serine proteases, trypsin family, histidine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / 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 / SYNCHROTRON / Resolution : 1.65 Å DetailsAuthors Wang, R. / Soares, A.S. / Radisky, E.S. CitationJournal : J.Biol.Chem. / Year : 2014Title : Sequence and Conformational Specificity in Substrate Recognition: SEVERAL HUMAN KUNITZ PROTEASE INHIBITOR DOMAINS ARE SPECIFIC SUBSTRATES OF MESOTRYPSIN.Authors : Pendlebury, D. / Wang, R. / Henin, R.D. / Hockla, A. / Soares, A.S. / Madden, B.J. / Kazanov, M.D. / Radisky, E.S. History Deposition Jul 18, 2014 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Oct 15, 2014 Provider : repository / Type : Initial releaseRevision 1.1 Nov 12, 2014 Group : Database referencesRevision 1.2 Dec 10, 2014 Group : Database referencesRevision 1.3 Jul 29, 2020 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description / Source and taxonomy / Structure summary Category : chem_comp / citation ... chem_comp / citation / entity / entity_src_gen / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_oper_list / refine_hist / struct_conn / struct_site / struct_site_gen Item : _chem_comp.name / _chem_comp.type ... _chem_comp.name / _chem_comp.type / _citation.journal_id_CSD / _entity.pdbx_description / _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_entity_nonpoly.name / _pdbx_struct_oper_list.symmetry_operation / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein / _struct_conn.pdbx_role Description : Carbohydrate remediation / Provider : repository / Type : RemediationRevision 1.4 Dec 27, 2023 Group : Data collection / Database references / Structure summaryCategory : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 Item : _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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