6QGN

Crystal structure of APT1 bound to 2-Bromopalmitate

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
Membrane Protein Annotation: mpstruc

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6qgna_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d6qgnb_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d6qgnc_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d6qgnd_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	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	alpha/beta-Hydrolases	8032561	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032561	3000102	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	alpha/beta-Hydrolases	8032561	3000102	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	alpha/beta-Hydrolases	8032561	3000102	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	Hydrolase_4	e6qgnA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
B	Hydrolase_4	e6qgnB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
C	Hydrolase_4	e6qgnC1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
D	Hydrolase_4	e6qgnD1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (utative)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (utative)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (utative)
D	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02230	Phospholipase/Carboxylesterase (Abhydrolase_2)	Phospholipase/Carboxylesterase	This family consists of both phospholipases [1] and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases Pfam:PF00561 [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Acyl-protein thioesterase 1	hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity catalytic activity phospholipase activity lipase activity palmitoyl-(protein) hydrolase activity palmitoyl hydrolase activity catalytic activity, acting on a protein thiolester hydrolase activity lysophospholipase activity	fatty acid metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process cellular lipid metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process organic anion transport carboxylic acid transport fatty acid metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process cellular lipid metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process organic anion transport carboxylic acid transport transport lipid localization lipid transport establishment of localization organic acid transport localization monocarboxylic acid transport fatty acid transport macromolecule localization negative regulation of protein transport protein localization regulation of localization Golgi to plasma membrane transport establishment of protein localization nitrogen compound transport regulation of cellular process negative regulation of biological process establishment of protein localization to plasma membrane negative regulation of transport Golgi to plasma membrane protein transport vesicle-mediated transport cellular macromolecule localization regulation of biological process protein localization to cell periphery establishment of protein localization to membrane negative regulation of establishment of protein localization localization within membrane regulation of protein localization to cell periphery protein localization to membrane negative regulation of protein localization to membrane regulation of Golgi to plasma membrane protein transport negative regulation of Golgi to plasma membrane protein transport Golgi vesicle transport cellular localization post-Golgi vesicle-mediated transport regulation of protein localization negative regulation of protein localization to plasma membrane negative regulation of cellular process regulation of protein localization to membrane negative regulation of protein localization regulation of transport protein localization to plasma membrane biological regulation regulation of establishment of protein localization regulation of protein transport regulation of vesicle-mediated transport vesicle-mediated transport to the plasma membrane protein transport regulation of cellular localization negative regulation of protein localization to cell periphery regulation of protein localization to plasma membrane negative regulation of cellular catabolic process catabolic process macroautophagy autophagy regulation of autophagy negative regulation of cellular metabolic process cellular catabolic process aggrephagy process utilizing autophagic mechanism negative regulation of catabolic process negative regulation of aggrephagy negative regulation of metabolic process regulation of aggrephagy regulation of cellular metabolic process regulation of catabolic process negative regulation of macroautophagy regulation of macroautophagy negative regulation of autophagy regulation of cellular catabolic process regulation of metabolic process lipoprotein metabolic process macromolecule deacylation protein catabolic process macromolecule catabolic process protein deacylation macromolecule modification macromolecule depalmitoylation protein depalmitoylation macromolecule metabolic process protein metabolic process protein modification process lipoprotein catabolic process	membrane-bounded organelle intracellular anatomical structure nuclear membrane membrane nucleus cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle envelope organelle nuclear envelope organelle membrane extracellular exosome membrane-bounded organelle intracellular anatomical structure nuclear membrane membrane nucleus cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle envelope organelle nuclear envelope organelle membrane extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytoplasm cytosol cell periphery plasma membrane membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR050565	Acyl-protein thioesterase 1-2/Carboxylesterase-like	Family
A, B, C, D	IPR003140	Phospholipase/carboxylesterase/thioesterase	Domain
A, B, C, D	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: O75608	Sjogren syndrome breast carcinoma hereditary spastic paraplegia large cell medulloblastoma malignant glioma pancreatic intraductal papillary-mucinous carcinoma Pick disease psoriasis ductal breast carcinoma in situ IgA glomerulonephritis lung adenocarcinoma osteosarcoma pancreatic intraductal papillary-mucinous neoplasm plasma cell myeloma rheumatoid arthritis Sjogren syndrome breast carcinoma hereditary spastic paraplegia large cell medulloblastoma malignant glioma pancreatic intraductal papillary-mucinous carcinoma Pick disease psoriasis ductal breast carcinoma in situ IgA glomerulonephritis lung adenocarcinoma osteosarcoma pancreatic intraductal papillary-mucinous neoplasm plasma cell myeloma rheumatoid arthritis glioblastoma invasive ductal breast carcinoma lung cancer ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia primitive neuroectodermal tumor

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C, D	mpstruc	MONOTOPIC MEMBRANE PROTEINS	Thioesterases	acyl protein thioesterase 1 (APT 1) bound to palmitic acid

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.