6AS8

F9 pilus adhesin FmlH lectin domain from E. coli UTI89 co-crystallized with ortho-biphenyl-2'-carboxyl N-acetyl-beta-galactosaminoside

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d6as8b_	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	automated matches	automated matches	(Escherichia coli UTI89 ) [TaxId: 364106 ],	SCOPe (2.08)
A	d6as8a_	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	automated matches	automated matches	(Escherichia coli UTI89 ) [TaxId: 364106 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Bacterial adhesin-like	8099224	3000723	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Bacterial adhesin-like	8099224	3000723	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	FimH_man-bind	e6as8B1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: FimH_man-bind	ECOD (1.6)
A	FimH_man-bind	e6as8A1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: FimH_man-bind	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.60.40.1090	Mainly Beta	Sandwich	Immunoglobulin-like	Fimbrial-type adhesion domain	CATH (4.3.0)
A	2.60.40.1090	Mainly Beta	Sandwich	Immunoglobulin-like	Fimbrial-type adhesion domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF09160	FimH, mannose binding (FimH_man-bind)	FimH, mannose binding	Members of this family adopt a secondary structure consisting of a beta sandwich, with nine strands arranged in two sheets in a Greek key topology. They are predominantly found in bacterial mannose-specific adhesins, since they are capable of binding ...	Members of this family adopt a secondary structure consisting of a beta sandwich, with nine strands arranged in two sheets in a Greek key topology. They are predominantly found in bacterial mannose-specific adhesins, since they are capable of binding to D-mannose [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Fml fimbrial adhesin FmlD	-	cell adhesion involved in biofilm formation cell aggregation biofilm formation biological process involved in intraspecies interaction between organisms cell-substrate adhesion single-species biofilm formation aggregation of unicellular organisms submerged biofilm formation cell adhesion involved in single-species biofilm formation cell adhesion cellular process single-species submerged biofilm formation	pilus cell projection cellular anatomical structure

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036937	Fimbrial-type adhesion domain superfamily	Homologous Superfamily
A, B	IPR015243	FimH, mannose-binding domain	Domain
A, B	IPR050263	Bacterial Fimbrial Adherence	Family
A, B	IPR008966	Adhesion domain superfamily	Homologous Superfamily

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.