Entry Database : PDB / ID : 3edz Structure visualization Downloads & linksTitle Crystal structure of catalytic domain of TACE with hydroxamate inhibitor ComponentsADAM 17 Details Keywords HYDROLASE / ZN-ENDOPEPTIDASE / Cleavage on pair of basic residues / Glycoprotein / Membrane / Metal-binding / Metalloprotease / Notch signaling pathway / Phosphoprotein / Protease / SH3-binding / Transmembrane / ZymogenFunction / homology Function and homology informationFunction Domain/homology Component
ADAM 17 endopeptidase / regulation of mast cell apoptotic process / signal release / metalloendopeptidase activity involved in amyloid precursor protein catabolic process / cellular response to high density lipoprotein particle stimulus / positive regulation of epidermal growth factor-activated receptor activity / Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant / tumor necrosis factor binding / interleukin-6 receptor binding / Notch receptor processing ... ADAM 17 endopeptidase / regulation of mast cell apoptotic process / signal release / metalloendopeptidase activity involved in amyloid precursor protein catabolic process / cellular response to high density lipoprotein particle stimulus / positive regulation of epidermal growth factor-activated receptor activity / Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant / tumor necrosis factor binding / interleukin-6 receptor binding / Notch receptor processing / positive regulation of T cell chemotaxis / TNF signaling / positive regulation of leukocyte chemotaxis / germinal center formation / Regulated proteolysis of p75NTR / Release of Hh-Np from the secreting cell / commissural neuron axon guidance / positive regulation of tumor necrosis factor-mediated signaling pathway / neutrophil mediated immunity / wound healing, spreading of epidermal cells / negative regulation of cold-induced thermogenesis / Notch binding / CD163 mediating an anti-inflammatory response / positive regulation of vascular endothelial cell proliferation / cell adhesion mediated by integrin / positive regulation of epidermal growth factor receptor signaling pathway / Signaling by EGFR / cytokine binding / amyloid precursor protein catabolic process / Collagen degradation / membrane protein ectodomain proteolysis / positive regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of blood vessel endothelial cell migration / positive regulation of G1/S transition of mitotic cell cycle / Growth hormone receptor signaling / Nuclear signaling by ERBB4 / positive regulation of chemokine production / spleen development / Notch signaling pathway / Constitutive Signaling by NOTCH1 HD Domain Mutants / B cell differentiation / Activated NOTCH1 Transmits Signal to the Nucleus / cell motility / PDZ domain binding / negative regulation of transforming growth factor beta receptor signaling pathway / protein processing / metalloendopeptidase activity / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / SH3 domain binding / positive regulation of tumor necrosis factor production / metallopeptidase activity / actin cytoskeleton / integrin binding / peptidase activity / T cell differentiation in thymus / positive regulation of cell growth / endopeptidase activity / response to lipopolysaccharide / response to hypoxia / cell adhesion / defense response to Gram-positive bacterium / positive regulation of cell migration / response to xenobiotic stimulus / apical plasma membrane / membrane raft / endoplasmic reticulum lumen / Golgi membrane / positive regulation of cell population proliferation / cell surface / proteolysis / membrane / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function ADAM17, membrane-proximal domain / Membrane-proximal domain, switch, for ADAM17 / Metallo-peptidase family M12 / ADAM10/ADAM17 catalytic domain / : / Disintegrin / Disintegrin domain profile. / Homologues of snake disintegrins / Disintegrin domain / Disintegrin domain superfamily ... ADAM17, membrane-proximal domain / Membrane-proximal domain, switch, for ADAM17 / Metallo-peptidase family M12 / ADAM10/ADAM17 catalytic domain / : / Disintegrin / Disintegrin domain profile. / Homologues of snake disintegrins / Disintegrin domain / Disintegrin domain superfamily / Peptidase M12B, ADAM/reprolysin / ADAM type metalloprotease domain profile. / Collagenase (Catalytic Domain) / Collagenase (Catalytic Domain) / Metallopeptidase, catalytic domain superfamily / Neutral zinc metallopeptidases, zinc-binding region signature. / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology 3,N(D,L-[2-(HYDROXYAMINO-CARBONYL)METHYL]-4-METHYL PENTANOYL)L-3-(TERT-BUTYL)GLYCYL-L-ALANINE / Chem-550 / CITRIC ACID / Chem-INN / Disintegrin and metalloproteinase domain-containing protein 17 Similarity search - ComponentBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / PDB entry 1bkc / Resolution : 1.9 Å DetailsAuthors Mazzola, R.D. / Zhu, Z. / Sinning, L. / McKittrick, B. / Lavey, B. / Spitler, J. / Kozlowski, J. / Neng-Yang, S. / Zhou, G. / Guo, Z. ...Mazzola, R.D. / Zhu, Z. / Sinning, L. / McKittrick, B. / Lavey, B. / Spitler, J. / Kozlowski, J. / Neng-Yang, S. / Zhou, G. / Guo, Z. / Orth, P. / Madison, V. / Sun, J. / Lundell, D. / Niu, X. CitationJournal : Bioorg.Med.Chem.Lett. / Year : 2008Title : Discovery of novel hydroxamates as highly potent tumor necrosis factor-alpha converting enzyme inhibitors. Part II: optimization of the S3' pocket.Authors : Mazzola, R.D. / Zhu, Z. / Sinning, L. / McKittrick, B. / Lavey, B. / Spitler, J. / Kozlowski, J. / Neng-Yang, S. / Zhou, G. / Guo, Z. / Orth, P. / Madison, V. / Sun, J. / Lundell, D. / Niu, X. History Deposition Sep 3, 2008 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Sep 23, 2008 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Non-polymer description / Version format complianceRevision 1.2 Feb 27, 2013 Group : OtherRevision 1.3 Oct 20, 2021 Group : Database references / Derived calculationsCategory : database_2 / pdbx_struct_conn_angle ... database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / 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_asym_id / _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_asym_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_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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