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Crystal structure of the ferripyoverdine receptor of the outer membrane of Pseudomonas aeruginosa bound to ferripyoverdine. External Resource: Annotation Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2B Superfamily STN domain-like 8057237 3002388 SCOP2B (2022-06-29) A SCOP2B Superfamily Porins 8057240 3000224 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A TonB_dep_Rec_1 e2iahA3 A: beta barrels X: Outer membrane meander beta-barrels H: Porins T: Ligand-gated protein channel F: TonB_dep_Rec_1 ECOD (1.6) A STN e2iahA1 A: a+b complex topology X: N0 domain in phage tail proteins and secretins-like H: N0 domain in phage tail proteins and secretins (From Topology) T: N0 domain in phage tail proteins and secretins F: STN ECOD (1.6) A Plug e2iahA2 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 PF07660 Secretin and TonB N terminus short domain (STN) Secretin and TonB N terminus short domain - Family 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 B [auth I] Pyoverdin C-E - - - Ferripyoverdine receptor
Protein Modification Annotation