Entry Database : PDB / ID : 4dd8 Structure visualization Downloads & linksTitle ADAM-8 metalloproteinase domain with bound batimastat ComponentsDisintegrin and metalloproteinase domain-containing protein 8 Details Keywords HYDROLASE/HYDROLASE INHIBITOR / batimastat / inflammation / alpha/beta motif / metalloproteinase / allergic asthma / tumorigenesis / arthritis / aberrant neural cell signaling / HYDROLASE-HYDROLASE INHIBITOR complexFunction / homology Function and homology informationFunction Domain/homology Component
positive regulation of fibronectin-dependent thymocyte migration / positive regulation of eosinophil migration / dense core granule membrane / tertiary granule / positive regulation of tumor necrosis factor (ligand) superfamily member 11 production / positive regulation of neutrophil extravasation / phagolysosome / neutrophil degranulation / positive regulation of T cell differentiation in thymus / regulation of cell-cell adhesion ... positive regulation of fibronectin-dependent thymocyte migration / positive regulation of eosinophil migration / dense core granule membrane / tertiary granule / positive regulation of tumor necrosis factor (ligand) superfamily member 11 production / positive regulation of neutrophil extravasation / phagolysosome / neutrophil degranulation / positive regulation of T cell differentiation in thymus / regulation of cell-cell adhesion / lymphocyte chemotaxis / alpha9-beta1 integrin-ADAM8 complex / positive regulation of protein processing / leukocyte migration involved in inflammatory response / positive regulation of acute inflammatory response / specific granule / positive regulation of innate immune response / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / podosome / positive regulation of membrane protein ectodomain proteolysis / positive regulation of thymocyte apoptotic process / plasma membrane => GO:0005886 / tertiary granule membrane / ficolin-1-rich granule membrane / positive regulation of cell adhesion / extracellular matrix disassembly / positive regulation of bone resorption / specific granule membrane / cell adhesion molecule binding / Degradation of the extracellular matrix / : / positive regulation of protein secretion / positive regulation of MAP kinase activity / cell morphogenesis / metalloendopeptidase activity / cell-cell adhesion / metallopeptidase activity / positive regulation of NF-kappaB transcription factor activity / cellular response to hypoxia / angiogenesis / negative regulation of neuron apoptotic process / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / inflammatory response / serine-type endopeptidase activity / calcium ion binding / Neutrophil degranulation / cell surface / zinc ion binding / plasma membrane / cytoplasm Similarity search - Function ADAM cysteine-rich / ADAM, cysteine-rich domain / ADAM Cysteine-Rich Domain / Disintegrin, conserved site / Disintegrins signature. / Peptidase M12B, propeptide / Reprolysin family propeptide / Reprolysin domain, adamalysin-type / Reprolysin (M12B) family zinc metalloprotease / Disintegrin ... ADAM cysteine-rich / ADAM, cysteine-rich domain / ADAM Cysteine-Rich Domain / Disintegrin, conserved site / Disintegrins signature. / Peptidase M12B, propeptide / Reprolysin family propeptide / Reprolysin domain, adamalysin-type / Reprolysin (M12B) family zinc metalloprotease / 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 / EGF-like domain profile. / EGF-like domain signature 2. / EGF-like domain / Neutral zinc metallopeptidases, zinc-binding region signature. / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.1 Å DetailsAuthors Hall, T. / Shieh, H.S. / Day, J.E. / Caspers, N. / Chrencik, J.E. / Williams, J.M. / Pegg, L.E. / Pauley, A.M. / Moon, A.F. / Krahn, J.M. ...Hall, T. / Shieh, H.S. / Day, J.E. / Caspers, N. / Chrencik, J.E. / Williams, J.M. / Pegg, L.E. / Pauley, A.M. / Moon, A.F. / Krahn, J.M. / Fischer, D.H. / Kiefer, J.R. / Tomasselli, A.G. / Zack, M.D. CitationJournal : Acta Crystallogr.,Sect.F / Year : 2012Title : Structure of human ADAM-8 catalytic domain complexed with batimastat.Authors : Hall, T. / Shieh, H.S. / Day, J.E. / Caspers, N. / Chrencik, J.E. / Williams, J.M. / Pegg, L.E. / Pauley, A.M. / Moon, A.F. / Krahn, J.M. / Fischer, D.H. / Kiefer, J.R. / Tomasselli, A.G. / Zack, M.D. History Deposition Jan 18, 2012 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jun 6, 2012 Provider : repository / Type : Initial releaseRevision 1.1 Jun 27, 2012 Group : Database referencesRevision 1.2 Sep 13, 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 / pdbx_struct_conn_angle / 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_asym_id / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Show all Show less