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Crystal structure of the siderophore receptor PirA from Acinetobacter baumannii External Resource: Annotation Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2 Family Ligand-gated protein channel 8072642 4003084 SCOP2 (2022-06-29) A SCOP2 Superfamily Porins 8072643 3000224 SCOP2 (2022-06-29) B SCOP2B Superfamily Porins 8072643 3000224 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A TonB_dep_Rec e5fr8A2 A: beta barrels X: Outer membrane meander beta-barrels H: Porins T: Ligand-gated protein channel F: TonB_dep_Rec ECOD (1.6) A Plug e5fr8A1 A: a+b complex topology X: N0 domain in phage tail proteins and secretins-like H: TonB-dependent receptor plug domain (From Topology) T: TonB-dependent receptor plug domain F: Plug ECOD (1.6) B TonB_dep_Rec e5fr8B2 A: beta barrels X: Outer membrane meander beta-barrels H: Porins T: Ligand-gated protein channel F: TonB_dep_Rec ECOD (1.6) B Plug e5fr8B1 A: a+b complex topology X: N0 domain in phage tail proteins and secretins-like H: TonB-dependent receptor plug domain (From Topology) T: TonB-dependent receptor plug domain F: Plug ECOD (1.6)
Chains Accession Name Description Comments Source PF00593 TonB dependent receptor-like, beta-barrel (TonB_dep_Rec_b-barrel) TonB dependent receptor-like, beta-barrel This entry represents the beta-barrel domain of TonB-dependent receptors, such as BtuB, CirA, FatA, FcuT, FecA, FepA, among others [1]. Domain PF07715 TonB-dependent Receptor Plug Domain (Plug) TonB-dependent Receptor Plug Domain The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors ([1]). It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens ... The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors ([1]). It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel. Less Domain
Chains Polymer Molecular Function Biological Process Cellular Component TONB-DEPENDENT SIDEROPHORE RECEPTOR -