5FQ6

Crystal structure of the SusCD complex BT2261-2264 from Bacteroides thetaiotaomicron

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: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
E	SCOP2B Superfamily	BT_2261-like	8106401	3002850	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	BT_2261-like	8106401	3002850	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	BT_2261-like	8106401	3002850	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	BT_2261-like	8106401	3002850	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)
A	SusD-like	e5fq6A1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: SusD-like	ECOD (1.6)
C	SusD-like	e5fq6C1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: SusD-like	ECOD (1.6)
H	SusD-like	e5fq6H1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: SusD-like	ECOD (1.6)
L	SusD-like	e5fq6L1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: SusD-like	ECOD (1.6)
B	TonB_dep_Rec_1	e5fq6B2	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	Plug	e5fq6B1	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)
D	TonB_dep_Rec_1	e5fq6D2	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Ligand-gated protein channel	F: TonB_dep_Rec_1	ECOD (1.6)
D	Plug	e5fq6D1	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)
I	TonB_dep_Rec_1	e5fq6I1	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Ligand-gated protein channel	F: TonB_dep_Rec_1	ECOD (1.6)
I	Plug	e5fq6I2	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)
M	TonB_dep_Rec_1	e5fq6M2	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Ligand-gated protein channel	F: TonB_dep_Rec_1	ECOD (1.6)
M	Plug	e5fq6M1	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)
E	Lipid_bd	e5fq6E1	A: beta barrels	X: Lipocalins/Streptavidin	H: Putative lipid binding protein BT_2261 (From Topology)	T: Putative lipid binding protein BT_2261	F: Lipid_bd	ECOD (1.6)
F	Lipid_bd	e5fq6F1	A: beta barrels	X: Lipocalins/Streptavidin	H: Putative lipid binding protein BT_2261 (From Topology)	T: Putative lipid binding protein BT_2261	F: Lipid_bd	ECOD (1.6)
J	Lipid_bd	e5fq6J1	A: beta barrels	X: Lipocalins/Streptavidin	H: Putative lipid binding protein BT_2261 (From Topology)	T: Putative lipid binding protein BT_2261	F: Lipid_bd	ECOD (1.6)
N	Lipid_bd	e5fq6N1	A: beta barrels	X: Lipocalins/Streptavidin	H: Putative lipid binding protein BT_2261 (From Topology)	T: Putative lipid binding protein BT_2261	F: Lipid_bd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.25.40.390	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat		CATH (4.3.0)
C	1.25.40.390	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat		CATH (4.3.0)
H	1.25.40.390	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat		CATH (4.3.0)
L	1.25.40.390	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat		CATH (4.3.0)
E	2.40.128.220	Mainly Beta	Beta Barrel	Lipocalin		CATH (4.3.0)
F	2.40.128.220	Mainly Beta	Beta Barrel	Lipocalin		CATH (4.3.0)
J	2.40.128.220	Mainly Beta	Beta Barrel	Lipocalin		CATH (4.3.0)
N	2.40.128.220	Mainly Beta	Beta Barrel	Lipocalin		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C, H, L	PF12771	Starch-binding associating with outer membrane (SusD-like_2)	Starch-binding associating with outer membrane	-	Repeat
B, D, I, M	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
E, F, J, N	PF12888	Lipid-binding putative hydrolase (Lipid_bd)	Lipid-binding putative hydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C, H, L	PUTATIVE LIPOPROTEIN	cation binding ion binding binding metal ion binding small molecule binding	-	-
B, D, I, M	SUSC/RAGA FAMILY TONB-LINKED OUTER MEMBRANE PROTEIN	cation binding ion binding binding metal ion binding small molecule binding	-	cell periphery cell outer membrane external encapsulating structure membrane cell envelope outer membrane cellular anatomical entity
E, F, J, N	UNCHARACTERIZED PROTEIN	-	-	-
G, K, O, P	BT_2261	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C, H, L	IPR041662	SusD-like 2	Family
A, C, H, L	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
B, D, I, M	IPR037066	TonB-dependent receptor, plug domain superfamily	Homologous Superfamily
B, D, I, M	IPR023997	TonB-dependent outer membrane protein SusC/RagA, conserved site	Conserved Site
B, D, I, M	IPR036942	TonB-dependent receptor-like, beta-barrel domain superfamily	Homologous Superfamily
B, D, I, M	IPR023996	TonB-dependent outer membrane protein, SusC/RagA	Family
B, D, I, M	IPR012910	TonB-dependent receptor, plug domain	Domain
E, F, J, N	IPR024404	Lipid-binding, putative	Family
E, F, J, N	IPR038668	Lipid-binding superfamily	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D, E A, B, C, D, E, F, H, I, J, L, M, N	OPM	Transmembrane	Beta-barrel transmembrane	Ligand-gated protein channels (n=22,S=24)	Outer Membrane Receptor (OMR)

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F, H, I, J, L, M, N	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F, H, I, J, L, M, N	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C, D, E A, B, C, D, E, F, H, I, J, L, M, N	mpstruc	TRANSMEMBRANE PROTEINS: BETA-BARREL	Polysaccharide Utilization Proteins	SusCD complex BT2261-2264, space group P1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.