6DXW

Human N-acylethanolamine-hydrolyzing acid amidase (NAAA) precursor (C126A)

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	UNK_F_TYPE	e6dxwA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Penicillin acylase, catalytic domain	F: UNK_F_TYPE	ECOD (1.6)
B	UNK_F_TYPE	e6dxwB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Penicillin acylase, catalytic domain	F: UNK_F_TYPE	ECOD (1.6)
C	UNK_F_TYPE	e6dxwC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Penicillin acylase, catalytic domain	F: UNK_F_TYPE	ECOD (1.6)
D	UNK_F_TYPE	e6dxwD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Penicillin acylase, catalytic domain	F: UNK_F_TYPE	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.60.10	Alpha Beta	4-Layer Sandwich	Penicillin V Acylase	Chain A	CATH (utative)
B	3.60.60.10	Alpha Beta	4-Layer Sandwich	Penicillin V Acylase	Chain A	CATH (utative)
C	3.60.60.10	Alpha Beta	4-Layer Sandwich	Penicillin V Acylase	Chain A	CATH (utative)
D	3.60.60.10	Alpha Beta	4-Layer Sandwich	Penicillin V Acylase	Chain A	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF15508	beta subunit of N-acylethanolamine-hydrolyzing acid amidase (NAAA-beta)	beta subunit of N-acylethanolamine-hydrolyzing acid amidase	-	Family
A, B, C, D	PF02275	Linear amide C-N hydrolases, choloylglycine hydrolase family (CBAH)	Linear amide C-N hydrolases, choloylglycine hydrolase family	This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and aci ...	This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, Pfam:PF15508.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	N-acylethanolamine-hydrolyzing acid amidase	hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds N-(long-chain-acyl)ethanolamine deacylase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides fatty acid amide hydrolase activity transcription factor binding protein binding binding DNA-binding transcription factor binding N-acylsphingosine amidohydrolase activity	fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process lipid catabolic process catabolic process phosphatidylethanolamine metabolic process glycerophospholipid metabolic process fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process lipid catabolic process catabolic process phosphatidylethanolamine metabolic process glycerophospholipid metabolic process phospholipid metabolic process organophosphate metabolic process phosphate-containing compound metabolic process glycerolipid metabolic process amide metabolic process N-acylphosphatidylethanolamine metabolic process phosphorus metabolic process membrane lipid metabolic process polyol metabolic process sphingolipid metabolic process alcohol metabolic process sphingosine metabolic process sphingoid metabolic process diol metabolic process N-acylethanolamine metabolic process amine metabolic process ethanolamine-containing compound metabolic process biogenic amine metabolic process primary alcohol metabolic process	cellular anatomical structure membrane membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen lytic vacuole vacuolar lumen vacuole intracellular membrane-bounded organelle lysosomal lumen intracellular organelle lumen intracellular organelle organelle lumen organelle cellular anatomical structure membrane membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen lytic vacuole vacuolar lumen vacuole intracellular membrane-bounded organelle lysosomal lumen intracellular organelle lumen intracellular organelle organelle lumen organelle cytoplasm lysosome extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR029130	Acid ceramidase, N-terminal	Domain
A, B, C, D	IPR016699	Acid ceramidase-like	Family
A, B, C, D	IPR029132	Choloylglycine hydrolase/NAAA C-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: Q02083	acute myeloid leukemia lung carcinoma osteosarcoma Sjogren syndrome interstitial cystitis malignant colon neoplasm ovarian cancer tuberculosis lung cancer malignant mesothelioma pancreatic ductal adenocarcinoma ulcerative colitis

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.