4E2L | pdb_00004e2l

Crystal Structure of the periplasmic domain of mutant FepE LPS O-antigen chain length regulator protein

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	d4e2la_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
B	d4e2lb_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
C	d4e2lc_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
D	d4e2ld_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
E	d4e2le_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
F	d4e2lf_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
G	d4e2lg_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
H	d4e2lh_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	SCOPe (2.08)
I	d4e2li_	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial polysaccharide co-polymerase-like	FepE-like	automated matches	(Escherichia coli O157:H7 ) [TaxId: 83334 ], (Escherichia coli O157:H7 ) [TaxId: 83334 ],	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 polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (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)
D	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Bacterial polysaccharide co-polymerase-like	8038973	3000641	SCOP2B (2022-06-29)
I	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	e4e2lA1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
B	PRK10381	e4e2lB1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
C	PRK10381	e4e2lC1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
D	PRK10381	e4e2lD1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
E	PRK10381	e4e2lE1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
F	PRK10381	e4e2lF1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
G	PRK10381	e4e2lG1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
H	PRK10381	e4e2lH1	A: a+b two layers	X: Alpha-beta plaits	H: FepE-like (From Topology)	T: FepE-like	F: PRK10381	ECOD (1.6)
I	PRK10381	e4e2lI1	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)
D	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
D	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
E	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
E	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
F	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
F	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
G	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
G	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
H	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
H	1.10.287.210	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
I	3.30.1890.10	Alpha Beta	2-Layer Sandwich	Bacterial polysaccharide co-polymerase-like	FepE-like	CATH (4.3.0)
I	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, D, E A, B, C, D, E, F, G, H, I	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, D, E A, B, C, D, E, F, G, H, I	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, D, E A, B, C, D, E, F, G, H, I	IPR050445	Bacterial polysaccharide biosynthesis and export	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I	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.