6EQH

Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup C2221

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	d6eqha1	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Piscinibacter sakaiensis ) [TaxId: 1547922 ],	SCOPe (2.08)
A	d6eqha2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Piscinibacter sakaiensis ) [TaxId: 1547922 ],	SCOPe (2.08)
B	d6eqhb1	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Piscinibacter sakaiensis ) [TaxId: 1547922 ],	SCOPe (2.08)
B	d6eqhb2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Piscinibacter sakaiensis ) [TaxId: 1547922 ],	SCOPe (2.08)
C	d6eqhc_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Piscinibacter sakaiensis ) [TaxId: 1547922 ],	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	8085716	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8085716	3000102	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	alpha/beta-Hydrolases	8085716	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	e6eqhA1	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	e6eqhB1	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	e6eqhC1	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 (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01738	Dienelactone hydrolase family (DLH)	Dienelactone hydrolase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Poly(ethylene terephthalate) hydrolase	hydrolase activity, acting on ester bonds short-chain carboxylesterase activity carboxylic ester hydrolase activity acetylesterase activity hydrolase activity catalytic activity	cellular response to stimulus catabolic process response to stimulus cellular response to xenobiotic stimulus xenobiotic catabolic process xenobiotic metabolic process response to xenobiotic stimulus cellular response to chemical stimulus response to chemical metabolic process cellular process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR050261	FrsA esterase	Family
A, B, C	IPR002925	Dienelactone hydrolase	Domain
A, B, C	IPR029058	Alpha/Beta hydrolase fold	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.