Entry Database : PDB / ID : 4dlo Structure visualization Downloads & linksTitle Crystal structure of the GAIN and HormR domains of brain angiogenesis inhibitor 3 (BAI3) ComponentsBrain-specific angiogenesis inhibitor 3 Details Keywords SIGNALING PROTEIN / GAIN domain / includes GPS motif / autoproteolytic fold / extracellularFunction / homology Function and homology informationFunction Domain/homology Component
motor learning / maintenance of synapse structure / myoblast fusion / positive regulation of synapse assembly / neuron remodeling / regulation of dendrite morphogenesis / plasma membrane => GO:0005886 / negative regulation of angiogenesis / synaptic cleft / GTPase activator activity ... motor learning / maintenance of synapse structure / myoblast fusion / positive regulation of synapse assembly / neuron remodeling / regulation of dendrite morphogenesis / plasma membrane => GO:0005886 / negative regulation of angiogenesis / synaptic cleft / GTPase activator activity / G protein-coupled receptor activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / postsynapse / membrane => GO:0016020 / cell surface receptor signaling pathway / G protein-coupled receptor signaling pathway / plasma membrane Similarity search - Function Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #610 / Chondroitinase Ac; Chain A, domain 3 - #50 / GPCR, family 2, brain-specific angiogenesis inhibitor / GPCR, family 2, extracellular hormone receptor domain / GAIN domain, N-terminal / GPCR-Autoproteolysis INducing (GAIN) domain / Hormone receptor fold / Chondroitinase Ac; Chain A, domain 3 / GPCR proteolysis site, GPS, motif / GPS motif ... Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #610 / Chondroitinase Ac; Chain A, domain 3 - #50 / GPCR, family 2, brain-specific angiogenesis inhibitor / GPCR, family 2, extracellular hormone receptor domain / GAIN domain, N-terminal / GPCR-Autoproteolysis INducing (GAIN) domain / Hormone receptor fold / Chondroitinase Ac; Chain A, domain 3 / GPCR proteolysis site, GPS, motif / GPS motif / GAIN-B domain profile. / G-protein-coupled receptor proteolytic site domain / CUB domain / CUB domain profile. / Thrombospondin type 1 domain / Thrombospondin type-1 (TSP1) repeat superfamily / Thrombospondin type-1 (TSP1) repeat profile. / Thrombospondin type 1 repeats / Thrombospondin type-1 (TSP1) repeat / Hormone receptor domain / GPCR, family 2, extracellular hormone receptor domain / G-protein coupled receptors family 2 profile 1. / Domain present in hormone receptors / GPCR family 2, extracellular hormone receptor domain superfamily / G-protein coupled receptors family 2 signature 2. / GPCR, family 2, secretin-like, conserved site / GPCR, family 2, secretin-like / 7 transmembrane receptor (Secretin family) / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Few Secondary Structures / Irregular / Alpha Horseshoe / Sandwich / Mainly Beta / Mainly Alpha Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution : 2.3 Å DetailsAuthors Arac, D. / Boucard, A.A. / Bolliger, M.F. / Nguyen, J. / Soltis, M. / Sudhof, T.C. / Brunger, A.T. CitationJournal : Embo J. / Year : 2012Title : A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.Authors : Arac, D. / Boucard, A.A. / Bolliger, M.F. / Nguyen, J. / Soltis, S.M. / Sudhof, T.C. / Brunger, A.T. History Deposition Feb 6, 2012 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Feb 22, 2012 Provider : repository / Type : Initial releaseRevision 1.1 Apr 4, 2012 Group : Database referencesRevision 1.2 Jul 16, 2014 Group : Refinement descriptionRevision 2.0 Jul 29, 2020 Group : Atomic model / Data collection ... Atomic model / Data collection / Database references / Derived calculations / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen Item : _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ... _atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_comp_id / _struct_ref_seq_dif.details Description : Carbohydrate remediation / Provider : repository / Type : Remediation
Show all Show less