1PP4

The crystal structure of rhamnogalacturonan acetylesterase in space group P3121

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1pp4a_	Alpha and beta proteins (a/b)	Flavodoxin-like	SGNH hydrolase	Rhamnogalacturonan acetylesterase	Rhamnogalacturonan acetylesterase	(Aspergillus aculeatus ) [TaxId: 5053 ],	SCOPe (2.08)
B	d1pp4b_	Alpha and beta proteins (a/b)	Flavodoxin-like	SGNH hydrolase	Rhamnogalacturonan acetylesterase	Rhamnogalacturonan acetylesterase	(Aspergillus aculeatus ) [TaxId: 5053 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	SGNH hydrolase-like	8037865	3001315	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SGNH hydrolase-like	8037865	3001315	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	Lipase_GDSL_2	e1pp4A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: SGNH hydrolase (From Topology)	T: SGNH hydrolase	F: Lipase_GDSL_2	ECOD (1.6)
B	Lipase_GDSL_2	e1pp4B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: SGNH hydrolase (From Topology)	T: SGNH hydrolase	F: Lipase_GDSL_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	SGNH hydrolase	CATH (4.3.0)
B	3.40.50.1110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	SGNH hydrolase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00657	GDSL-like Lipase/Acylhydrolase (Lipase_GDSL)	GDSL-like Lipase/Acylhydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Rhamnogalacturonan acetylesterase	hydrolase activity, acting on ester bonds hydrolase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001087	GDSL lipase/esterase	Family
A, B	IPR036514	SGNH hydrolase superfamily	Homologous Superfamily
A, B	IPR037459	Rhamnogalacturonan acetylesterase RhgT-like	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	rhamnogalacturonan acetylesterase M-CSA #705	Rhamnogalacturonan acetyltransferase (RGAE) is one of a group of enzymes produced by Aspergillus aculeatus to perform the synergistic degradation of rhamnogalacturonan, a complex polysaccharide found in pectic substances that constitute part of the middle lamella and the primary cell wall of higher plants. RGAE catalyses the deacylation of the backbone of rhamnogalacturonan, which is essential for the subsequent action of enzymes that cleave the glycosidic bonds and so degrade the polysaccharide. RGAE is a member of the carbohydrate esterase family 12, performing hydrolysis on an ester bond using a Ser-His-Asp catalytic triad.	Defined by 5 residues: SER:A-9GLY:A-42ASN:A-74ASP:A-192HIS:A-195 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.1 (PDB Primary Data) Search M-CSA Motif + EC 3.1.1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.