Entry Database : PDB / ID : 3c7x Structure visualization Downloads & linksTitle Hemopexin-like domain of matrix metalloproteinase 14 ComponentsMatrix metalloproteinase-14 Details Keywords HYDROLASE / membrane protein interaction / pro-MMP-2 / TIMP-2 / metastasis / Cleavage on pair of basic residues / Metal-binding / Metalloprotease / Protease / Transmembrane / ZymogenFunction / homology Function and homology informationFunction Domain/homology Component
membrane-type matrix metalloproteinase-1 / craniofacial suture morphogenesis / positive regulation of macrophage migration / macropinosome / head development / chondrocyte proliferation / astrocyte cell migration / response to odorant / tissue remodeling / negative regulation of focal adhesion assembly ... membrane-type matrix metalloproteinase-1 / craniofacial suture morphogenesis / positive regulation of macrophage migration / macropinosome / head development / chondrocyte proliferation / astrocyte cell migration / response to odorant / tissue remodeling / negative regulation of focal adhesion assembly / positive regulation of protein processing / endochondral ossification / embryonic cranial skeleton morphogenesis / zymogen activation / endothelial cell proliferation / intermediate filament cytoskeleton / positive regulation of B cell differentiation / branching morphogenesis of an epithelial tube / positive regulation of myotube differentiation / negative regulation of Notch signaling pathway / Activation of Matrix Metalloproteinases / endodermal cell differentiation / metalloaminopeptidase activity / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / regulation of protein localization to plasma membrane / response to mechanical stimulus / ovarian follicle development / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / skeletal system development / cell motility / lung development / response to organic cyclic compound / protein processing / metalloendopeptidase activity / Golgi lumen / response to estrogen / male gonad development / melanosome / integrin binding / cytoplasmic vesicle / positive regulation of cell growth / angiogenesis / endopeptidase activity / response to oxidative stress / response to hypoxia / positive regulation of cell migration / serine-type endopeptidase activity / focal adhesion / proteolysis / extracellular space / zinc ion binding / nucleus / plasma membrane / cytosol Similarity search - Function Peptidase M10A, matrix metallopeptidase, C-terminal / Domain of unknown function (DUF3377) / 4 Propeller / Hemopexin / Hemopexin-like domain / PGBD superfamily / Peptidoglycan binding-like / Hemopexin, conserved site / Hemopexin domain signature. / Hemopexin-like domain ... Peptidase M10A, matrix metallopeptidase, C-terminal / Domain of unknown function (DUF3377) / 4 Propeller / Hemopexin / Hemopexin-like domain / PGBD superfamily / Peptidoglycan binding-like / Hemopexin, conserved site / Hemopexin domain signature. / Hemopexin-like domain / Peptidase M10A, cysteine switch, zinc binding site / Matrixins cysteine switch. / Putative peptidoglycan binding domain / Hemopexin-like repeats / Hemopexin-like domain superfamily / Hemopexin / Hemopexin repeat profile. / Hemopexin-like repeats. / Peptidase M10A / Peptidase M10A, catalytic domain / Peptidase M10, metallopeptidase / Matrixin / PGBD-like superfamily / Peptidase, metallopeptidase / Zinc-dependent metalloprotease / Metallopeptidase, catalytic domain superfamily / Neutral zinc metallopeptidases, zinc-binding region signature. / Mainly Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.7 Å DetailsAuthors Tochowicz, A. / Itoh, Y. / Maskos, K. / Bode, W. / Goettig, P. CitationJournal : J.Biol.Chem. / Year : 2011Title : The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functionsAuthors : Tochowicz, A. / Goettig, P. / Evans, R. / Visse, R. / Shitomi, Y. / Palmisano, R. / Ito, N. / Richter, K. / Maskos, K. / Franke, D. / Svergun, D. / Nagase, H. / Bode, W. / Itoh, Y. History Deposition Feb 8, 2008 Deposition site : RCSB / Processing site : PDBJRevision 1.0 Feb 10, 2009 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Version format complianceRevision 1.2 Dec 26, 2012 Group : Database referencesRevision 1.3 Jun 20, 2018 Group : Advisory / Data collection / Source and taxonomy / Category : entity_src_gen / pdbx_unobs_or_zero_occ_atomsItem : _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strainRevision 1.4 Nov 1, 2023 Group : Advisory / Data collection ... Advisory / 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 / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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