2Q51

Ensemble refinement of the protein crystal structure of an aspartoacylase from Homo sapiens

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
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2q51a_	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	AstE/AspA-like	Aspartoacylase AspA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2q51b_	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	AstE/AspA-like	Aspartoacylase AspA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Zn-dependent exopeptidases	8034373	3000662	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8034373	3000662	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	AstE_AspA_C_1	e2q51A3	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: Succinylglutamate desuccinylase / Aspartoacylase C-terminal domain (From Topology)	T: Succinylglutamate desuccinylase / Aspartoacylase C-terminal domain	F: AstE_AspA_C_1	ECOD (1.6)
A	AstE_AspA_N	e2q51A2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: AstE_AspA_N	ECOD (1.6)
B	AstE_AspA_C_1	e2q51B3	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: Succinylglutamate desuccinylase / Aspartoacylase C-terminal domain (From Topology)	T: Succinylglutamate desuccinylase / Aspartoacylase C-terminal domain	F: AstE_AspA_C_1	ECOD (1.6)
B	AstE_AspA_N	e2q51B2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: AstE_AspA_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
A	2.20.25.160	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)
B	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
B	2.20.25.160	Mainly Beta	Single Sheet	N-terminal domain of TfIIb		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04952	AstE/AspA barrel-sandwich hybrid domain (AstE_AspA_hybrid)	Succinylglutamate desuccinylase / Aspartoacylase family	This family includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyses the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate ...	This family includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyses the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate into a fatty acid and aspartate. Mutations in Swiss:P45381 lead to Canavan disease disease [1]. This family is probably structurally related to Pfam:PF00246 (Bateman A pers. obs.).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Aspartoacylase	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides aspartoacylase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds hydrolase activity, acting on ester bonds cation binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding	oxoacid metabolic process carboxylic acid metabolic process acetate metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process organic acid metabolic process dicarboxylic acid metabolic process aspartate family amino acid metabolic process amino acid metabolic process primary metabolic process alpha-amino acid metabolic process L-amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process acetate metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process organic acid metabolic process dicarboxylic acid metabolic process aspartate family amino acid metabolic process amino acid metabolic process primary metabolic process alpha-amino acid metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process aspartate metabolic process developmental process multicellular organismal process oligodendrocyte development cellular developmental process central nervous system myelination cell development nervous system development glial cell development myelination multicellular organism development neurogenesis axon ensheathment in central nervous system central nervous system development gliogenesis oligodendrocyte differentiation glial cell differentiation axon ensheathment ensheathment of neurons cell differentiation anatomical structure development system development positive regulation of nervous system development regulation of cellular process regulation of developmental process positive regulation of biological process regulation of cell differentiation regulation of neurogenesis regulation of gliogenesis positive regulation of gliogenesis regulation of cell development regulation of nervous system development positive regulation of developmental process positive regulation of cell differentiation regulation of multicellular organismal process positive regulation of neurogenesis positive regulation of cellular process positive regulation of oligodendrocyte differentiation regulation of biological process regulation of multicellular organismal development regulation of glial cell differentiation biological regulation positive regulation of cell development positive regulation of glial cell differentiation positive regulation of multicellular organismal process regulation of oligodendrocyte differentiation	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR016708	Aspartoacylase	Family
A, B	IPR007036	AstE/AspA barrel-sandwich hybrid domain	Domain
A, B	IPR050178	AspA/AstE family	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P45381	Canavan disease leukodystrophy large cell medulloblastoma lung cancer malignant glioma mild Canavan disease adrenal cortex carcinoma osteosarcoma atopic eczema pancreatic intraductal papillary-mucinous neoplasm breast carcinoma pilocytic astrocytoma psoriasis Canavan Disease, Familial Form ulcerative colitis Canavan disease leukodystrophy large cell medulloblastoma lung cancer malignant glioma mild Canavan disease adrenal cortex carcinoma osteosarcoma atopic eczema pancreatic intraductal papillary-mucinous neoplasm breast carcinoma pilocytic astrocytoma psoriasis Canavan Disease, Familial Form ulcerative colitis ductal breast carcinoma in situ intellectual disability lung carcinoma MALT lymphoma non-small cell lung carcinoma ovarian cancer atypical teratoid rhabdoid tumor pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia primitive neuroectodermal tumor breast fibroadenoma severe Canavan disease invasive ductal breast carcinoma lung adenocarcinoma malignant colon neoplasm medulloblastoma oligodendroglioma astrocytic tumor pancreatic intraductal papillary-mucinous carcinoma breast cancer Pick disease progressive supranuclear palsy transitional cell carcinoma Down syndrome glioblastoma

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.