2W76

Structures of P. aeruginosa FpvA bound to heterologous pyoverdines: FpvA-Pvd(Pa6)-Fe complex

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Porins	8057240	3000224	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	STN domain-like	8057237	3002388	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	STN domain-like	8057237	3002388	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Porins	8057240	3000224	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	TonB_dep_Rec_1	e2w76B1	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Ligand-gated protein channel	F: TonB_dep_Rec_1	ECOD (1.6)
B	STN	e2w76B3	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)
B	Plug	e2w76B4	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)
A	TonB_dep_Rec_1	e2w76A3	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	e2w76A2	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	e2w76A4	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.55.50.30	Alpha Beta	3-Layer(bab) Sandwich	Phage tail protein beta-alpha-beta fold		CATH (4.3.0)
B	2.170.130.10	Mainly Beta	Beta Complex	Ferric Hydroxamate Uptake Protein	Chain A, domain 1	CATH (4.3.0)
B	2.40.170.20	Mainly Beta	Beta Barrel	Maltoporin	Chain A	CATH (4.3.0)
A	3.55.50.30	Alpha Beta	3-Layer(bab) Sandwich	Phage tail protein beta-alpha-beta fold		CATH (4.3.0)
A	2.170.130.10	Mainly Beta	Beta Complex	Ferric Hydroxamate Uptake Protein	Chain A, domain 1	CATH (4.3.0)
A	2.40.170.20	Mainly Beta	Beta Barrel	Maltoporin	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07660	Secretin and TonB N terminus short domain (STN)	Secretin and TonB N terminus short domain	-	Family
A, B	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
A, B	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.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	FERRIPYOVERDINE RECEPTOR	molecular transducer activity signaling receptor activity siderophore-iron transmembrane transporter activity siderophore uptake transmembrane transporter activity transporter activity transmembrane transporter activity	amide biosynthetic process secondary metabolic process pyoverdine biosynthetic process siderophore biosynthetic process biosynthetic process peptide biosynthetic process secondary metabolite biosynthetic process siderophore metabolic process metabolic process cellular process amide metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	cellular anatomical structure membrane cell periphery cell outer membrane external encapsulating structure cell envelope outer membrane
C	PYOVERDIN R	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR039426	TonB-dependent receptor-like	Family
A, B	IPR037066	TonB-dependent receptor, plug domain superfamily	Homologous Superfamily
A, B	IPR010917	TonB-dependent receptor, conserved site	Conserved Site
A, B	IPR010105	TonB-dependent siderophore receptor	Family
A, B	IPR036942	TonB-dependent receptor-like, beta-barrel domain superfamily	Homologous Superfamily
A, B	IPR012910	TonB-dependent receptor, plug domain	Domain
A, B	IPR011662	Secretin/TonB, short N-terminal domain	Domain
A, B	IPR000531	TonB-dependent receptor-like, beta-barrel	Domain

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B	MemProtMD	Annotated as membrane protein by MemProtMD

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C	DAB	Parent Component: ALA
C	DGN
C	DSN	RESID: AA0195 , AA0624 PSI-MOD : D-serine (Ser) MOD:00202 , D-serine MOD:00891 , D-serine (Cys) MOD:00892 , 2-(L-cystein-S-yl)-D-serine MOD:01987
C	FHO	Parent Component: LYS RESID: AA0195 , AA0624

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.