3B8M | pdb_00003b8m

Structure of FepE- Bacterial Polysaccharide Co-polymerase

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	d3b8ma1	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	Enterochelin transport protein FepE	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d3b8mb_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	Enterochelin transport protein FepE	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d3b8mc_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	Enterochelin transport protein FepE	(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	SCOP2 Family	FepE-like	8026594	4001984	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	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	PRK10381	e3b8mA1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
B	PRK10381	e3b8mB1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
C	PRK10381	e3b8mC1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
A	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
B	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
B	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
C	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
C	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF02706	Chain length determinant protein (Wzz)	Chain length determinant protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Ferric enterobactin (Enterochelin) transport	identical protein binding protein binding binding protein tyrosine kinase activity catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups	-	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR050445	Bacterial polysaccharide biosynthesis and export	Family
A, B, C	IPR003856	Polysaccharide chain length determinant N-terminal domain	Domain

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.