1P42

Crystal structure of Aquifex aeolicus LpxC Deacetylase (Zinc-Inhibited 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	d1p42a1	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase LpxC	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase LpxC	(Aquifex aeolicus ) [TaxId: 63363 ],	SCOPe (2.08)
B	d1p42b1	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase LpxC	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase LpxC	(Aquifex aeolicus ) [TaxId: 63363 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	UDP-3-O-(3-hydroxymyristoyl)N-acetylglucosamine deacetylase LpxC	8022213	4000578	SCOP2 (2022-06-29)
A	SCOP2 Family	UDP-3-O-(3-hydroxymyristoyl)N-acetylglucosamine deacetylase LpxC	8022214	4000578	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Ribosomal protein S5 domain 2-like	8034593	3000100	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Ribosomal protein S5 domain 2-like	8034594	3000100	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8034594	3000100	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8034593	3000100	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	LpxC	e1p42A1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: LpxC	ECOD (1.6)
A	UNK_F_TYPE	e1p42A2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: UNK_F_TYPE	ECOD (1.6)
B	LpxC	e1p42B1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: LpxC	ECOD (1.6)
B	UNK_F_TYPE	e1p42B2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: UNK_F_TYPE	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.230.20	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
A	3.30.1700.10	Alpha Beta	2-Layer Sandwich	lpxc deacetylase, domain 1	lpxc deacetylase, domain 2	CATH (4.3.0)
B	3.30.230.20	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
B	3.30.1700.10	Alpha Beta	2-Layer Sandwich	lpxc deacetylase, domain 1	lpxc deacetylase, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03331	UDP-3-O-acyl N-acetylglycosamine deacetylase (LpxC)	UDP-3-O-acyl N-acetylglycosamine deacetylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides UDP-3-O-acyl-N-acetylglucosamine deacetylase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding ion binding binding metal ion binding small molecule binding	glycolipid metabolic process cellular biosynthetic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process cellular metabolic process liposaccharide metabolic process glycolipid metabolic process cellular biosynthetic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process cellular metabolic process liposaccharide metabolic process primary metabolic process glycolipid biosynthetic process phospholipid biosynthetic process lipid A metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004463	UDP-3-O-acyl N-acetylglucosamine deacetylase	Family
A, B	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A, B	IPR015870	UDP-3-O-acyl N-acetylglucosamine deacetylase, N-terminal	Homologous Superfamily
A, B	IPR011334	UDP-3-O-acyl N-acetylglucosamine deacetylase, C-terminal	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.