2JKN

DraE Adhesin in complex with Chloramphenicol Succinate (trigonal form)

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)
A	d2jkna1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	Dr-family adhesin	DraA/Afimbrial adhesin Afa-III	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d2jkna2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d2jknb1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	Dr-family adhesin	DraA/Afimbrial adhesin Afa-III	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d2jknb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d2jknc1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	Dr-family adhesin	DraA/Afimbrial adhesin Afa-III	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d2jknc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d2jknd1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	Dr-family adhesin	DraA/Afimbrial adhesin Afa-III	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d2jknd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d2jkne1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	Dr-family adhesin	DraA/Afimbrial adhesin Afa-III	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d2jkne2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d2jknf1	All beta proteins	Common fold of diphtheria toxin/transcription factors/cytochrome f	Bacterial adhesins	Dr-family adhesin	DraA/Afimbrial adhesin Afa-III	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d2jknf2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(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)
A	SCOP2B Superfamily	Bacterial adhesin-like	8040901	3000723	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Bacterial adhesin-like	8040901	3000723	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Bacterial adhesin-like	8040901	3000723	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Bacterial adhesin-like	8040901	3000723	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Bacterial adhesin-like	8040901	3000723	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Bacterial adhesin-like	8040901	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)
A	Adhesin_Dr	e2jknA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Adhesin_Dr	ECOD (1.6)
B	Adhesin_Dr	e2jknB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Adhesin_Dr	ECOD (1.6)
C	Adhesin_Dr	e2jknC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Adhesin_Dr	ECOD (1.6)
D	Adhesin_Dr	e2jknD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Adhesin_Dr	ECOD (1.6)
E	Adhesin_Dr	e2jknE1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Adhesin_Dr	ECOD (1.6)
F	Adhesin_Dr	e2jknF1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Adhesin_Dr	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1570	Mainly Beta	Sandwich	Immunoglobulin-like	Dr adhesin	CATH (4.3.0)
B	2.60.40.1570	Mainly Beta	Sandwich	Immunoglobulin-like	Dr adhesin	CATH (4.3.0)
C	2.60.40.1570	Mainly Beta	Sandwich	Immunoglobulin-like	Dr adhesin	CATH (4.3.0)
D	2.60.40.1570	Mainly Beta	Sandwich	Immunoglobulin-like	Dr adhesin	CATH (4.3.0)
E	2.60.40.1570	Mainly Beta	Sandwich	Immunoglobulin-like	Dr adhesin	CATH (4.3.0)
F	2.60.40.1570	Mainly Beta	Sandwich	Immunoglobulin-like	Dr adhesin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF04619	Dr-family adhesin (Adhesin_Dr)	Dr-family adhesin	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	DR HEMAGGLUTININ STRUCTURAL SUBUNIT	-	-	pilus cell projection cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR037028	Dr-adhesin superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR006713	Adhesin, Dr-family	Family
A, B, C, D, E A, B, C, D, E, F	IPR008966	Adhesion domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR021020	Adhesin, Dr family, signal peptide	PTM

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.