Entry Database : PDB / ID : 6e4x Structure visualization Downloads & linksTitle Human antibody S5V2-29 in complex with influenza hemagglutinin A/Texas/50/2012 (H3N2) ComponentsHemagglutinin S5V2-29 heavy chain S5V2-29 light chain DetailsKeywords VIRAL PROTEIN/IMMUNE SYSTEM / influenza antibody / VIRAL PROTEIN-IMMUNE SYSTEM complexFunction / homology Function and homology informationFunction Domain/homology Component
viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / immune response / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane ... viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / immune response / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / extracellular space / metal ion binding Similarity search - Function Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Immunoglobulin V-Type ... Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Ribbon / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Alpha-Beta Complex / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homologyBiological species Influenza A virusHomo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.25 Å DetailsAuthors McCarthy, K.R. / Harrison, S.C. Funding support United States, 3items Details Hide detailsOrganization Grant number Country National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) P01AI089618 United States National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) 1U19AI117892-01 United States National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) AI128832 United States
CitationJournal : Cell / Year : 2019Title : Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism.Authors: Watanabe, A. / McCarthy, K.R. / Kuraoka, M. / Schmidt, A.G. / Adachi, Y. / Onodera, T. / Tonouchi, K. / Caradonna, T.M. / Bajic, G. / Song, S. / McGee, C.E. / Sempowski, G.D. / Feng, F. / ... Authors : Watanabe, A. / McCarthy, K.R. / Kuraoka, M. / Schmidt, A.G. / Adachi, Y. / Onodera, T. / Tonouchi, K. / Caradonna, T.M. / Bajic, G. / Song, S. / McGee, C.E. / Sempowski, G.D. / Feng, F. / Urick, P. / Kepler, T.B. / Takahashi, Y. / Harrison, S.C. / Kelsoe, G. History Deposition Jul 18, 2018 Deposition site : RCSB / Processing site : RCSBRevision 1.0 May 22, 2019 Provider : repository / Type : Initial releaseRevision 1.1 May 29, 2019 Group : Data collection / Database references / Category : citation / citation_authorItem : _citation.country / _citation.journal_abbrev ... _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title Revision 1.2 Dec 18, 2019 Group : Author supporting evidence / Data collection / Category : chem_comp / pdbx_audit_supportItem : _chem_comp.type / _pdbx_audit_support.funding_organizationRevision 2.0 Jul 29, 2020 Group : Atomic model / Data collection ... Atomic model / Data collection / Derived calculations / Structure summary Category : atom_site / chem_comp ... atom_site / 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_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 / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.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_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_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 Description : Carbohydrate remediation / Provider : repository / Type : Remediation
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