Entry Database : PDB / ID : 2wnp Structure visualization Downloads & linksTitle M-ficolin mutant Y271F ComponentsFICOLIN-1 Details Keywords IMMUNE SYSTEM / GLYCOPROTEIN / INNATE IMMUNITY / FIBRINOGEN-LIKE DOMAIN / CARBOHYDRATE RECOGNITION / LECTINFunction / homology Function and homology informationFunction Domain/homology Component
recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / cell surface pattern recognition receptor signaling pathway / complement activation, lectin pathway / sialic acid binding / negative regulation of viral entry into host cell / carbohydrate derivative binding / collagen trimer ... recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / cell surface pattern recognition receptor signaling pathway / complement activation, lectin pathway / sialic acid binding / negative regulation of viral entry into host cell / carbohydrate derivative binding / collagen trimer / protein localization to cell surface / serine-type endopeptidase complex / pattern recognition receptor activity / Initial triggering of complement / G protein-coupled receptor binding / positive regulation of interleukin-8 production / antigen binding / carbohydrate binding / secretory granule lumen / collagen-containing extracellular matrix / ficolin-1-rich granule lumen / G protein-coupled receptor signaling pathway / external side of plasma membrane / signaling receptor binding / Neutrophil degranulation / proteolysis / extracellular space / extracellular region / metal ion binding / plasma membrane Similarity search - Function Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2 / Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2 / Gamma Fibrinogen; Chain A, domain 1 / Gamma Fibrinogen, chain A, domain 1 / Fibrinogen, conserved site / Fibrinogen C-terminal domain signature. / Fibrinogen-related domains (FReDs) / Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 / Fibrinogen beta and gamma chains, C-terminal globular domain / Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain ... Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2 / Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2 / Gamma Fibrinogen; Chain A, domain 1 / Gamma Fibrinogen, chain A, domain 1 / Fibrinogen, conserved site / Fibrinogen C-terminal domain signature. / Fibrinogen-related domains (FReDs) / Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 / Fibrinogen beta and gamma chains, C-terminal globular domain / Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain / Fibrinogen-like, C-terminal / Fibrinogen C-terminal domain profile. / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / Few Secondary Structures / Irregular / Alpha-Beta Complex / Alpha Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.21 Å DetailsAuthors Gout, E. / Garlatti, V. / Smith, D.F. / Lacroix, M. / Dumestre-Perard, C. / Lunardi, T. / Arlaud, G.J. / Gaboriaud, C. / Thielens, N.M. CitationJournal : J.Biol.Chem. / Year : 2010Title : Carbohydrate Recognition Properties of Human Ficolins: Glycan Array Screening Reveals the Sialic Acid Binding Specificity of M-Ficolin.Authors : Gout, E. / Garlatti, V. / Smith, D.F. / Lacroix, M. / Dumestre-Perard, C. / Lunardi, T. / Martin, L. / Cesbron, J.Y. / Arlaud, G.J. / Gaboriaud, C. / Thielens, N.M. History Deposition Jul 16, 2009 Deposition site : PDBE / Processing site : PDBERevision 1.0 Dec 22, 2009 Provider : repository / Type : Initial releaseRevision 1.1 May 8, 2011 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / 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_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_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_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.