1AF6

MALTOPORIN SUCROSE COMPLEX

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
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: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1af6b_	Membrane and cell surface proteins and peptides	Transmembrane beta-barrels	Porins	Maltoporin-like	Maltoporin (also LamB protein)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1af6c_	Membrane and cell surface proteins and peptides	Transmembrane beta-barrels	Porins	Maltoporin-like	Maltoporin (also LamB protein)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1af6a_	Membrane and cell surface proteins and peptides	Transmembrane beta-barrels	Porins	Maltoporin-like	Maltoporin (also LamB protein)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Porins	8037890	3000224	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Porins	8037890	3000224	SCOP2B (2022-06-29)
A	SCOP2 Family	Maltoporin-like	8025511	4003069	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Porins	8037890	3000224	SCOP2 (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	LamB	e1af6B1	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Maltoporin-like	F: LamB	ECOD (1.6)
C	LamB	e1af6C1	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Maltoporin-like	F: LamB	ECOD (1.6)
A	LamB	e1af6A1	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Maltoporin-like	F: LamB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.40.170.10	Mainly Beta	Beta Barrel	Maltoporin	Chain A	CATH (4.3.0)
C	2.40.170.10	Mainly Beta	Beta Barrel	Maltoporin	Chain A	CATH (4.3.0)
A	2.40.170.10	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, C	PF02264	LamB porin (LamB)	LamB porin	Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	MALTOPORIN	protein binding binding virus receptor activity exogenous protein binding wide pore channel activity passive transmembrane transporter activity channel activity porin activity transporter activity transmembrane transporter activity carbohydrate transmembrane transporter activity macromolecule transmembrane transporter activity maltodextrin transmembrane transporter activity dextrin transmembrane transporter activity protein binding binding virus receptor activity exogenous protein binding wide pore channel activity passive transmembrane transporter activity channel activity porin activity transporter activity transmembrane transporter activity carbohydrate transmembrane transporter activity macromolecule transmembrane transporter activity maltodextrin transmembrane transporter activity dextrin transmembrane transporter activity polysaccharide transmembrane transporter activity disaccharide transmembrane transporter activity oligosaccharide transmembrane transporter activity maltose transmembrane transporter activity maltose transporting porin activity	cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process localization polysaccharide localization dextrin transport transport macromolecule localization maltodextrin transmembrane transport carbohydrate transport polysaccharide transport cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process localization polysaccharide localization dextrin transport transport macromolecule localization maltodextrin transmembrane transport carbohydrate transport polysaccharide transport establishment of localization monoatomic ion transport	protein-containing complex cellular anatomical structure membrane pore complex membrane protein complex cell periphery cell outer membrane external encapsulating structure cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR050286	Gram-negative Bacterial Carbohydrate Uptake Porin	Family
A, B, C	IPR003192	Porin, LamB-type	Family
A, B, C	IPR023738	Maltoporin	Family
A, B, C	IPR036998	Porin, LamB-type superfamily	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C	OPM	Transmembrane	Beta-barrel transmembrane	Sugar porins (n=18,S=22)	Malptoporin-like proteins

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

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

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

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

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C	mpstruc	TRANSMEMBRANE PROTEINS: BETA-BARREL	Beta-Barrel Membrane Proteins: Porins and Relatives	LamB Maltoporin in complex with sucrose

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.