2DVU

Crystal Structure of 2,6-Dihydroxybenzoate Decarboxylase Complexed with 2,6-Dihydroxybenzoate

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	d2dvua_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	PP1699/LP2961-like	Thermophilic reversible gamma-resorcylate decarboxylase	(Rhizobium sp. MTP-10005 ) [TaxId: 267998 ],	SCOPe (2.08)
C	d2dvuc_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	PP1699/LP2961-like	Thermophilic reversible gamma-resorcylate decarboxylase	(Rhizobium sp. MTP-10005 ) [TaxId: 267998 ],	SCOPe (2.08)
B	d2dvub_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	PP1699/LP2961-like	Thermophilic reversible gamma-resorcylate decarboxylase	(Rhizobium sp. MTP-10005 ) [TaxId: 267998 ],	SCOPe (2.08)
D	d2dvud_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Metallo-dependent hydrolases	PP1699/LP2961-like	Thermophilic reversible gamma-resorcylate decarboxylase	(Rhizobium sp. MTP-10005 ) [TaxId: 267998 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Metallo-dependent hydrolases	8039940	3000428	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Metallo-dependent hydrolases	8039940	3000428	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metallo-dependent hydrolases	8039940	3000428	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Metallo-dependent hydrolases	8039940	3000428	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	Amidohydro_2	e2dvuA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_2	ECOD (1.6)
C	Amidohydro_2	e2dvuC1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_2	ECOD (1.6)
B	Amidohydro_2	e2dvuB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_2	ECOD (1.6)
D	Amidohydro_2	e2dvuD1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Amidohydro_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
C	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
B	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
D	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF04909	Amidohydrolase (Amidohydro_2)	Amidohydrolase	These proteins are amidohydrolases that are related to Pfam:PF01979 [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Thermophilic reversible gamma-resorcylate decarboxylase	hydrolase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding carboxy-lyase activity lyase activity carbon-carbon lyase activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR032465	2-amino-3-carboxymuconate-6-semialdehyde decarboxylase	Family
A, B, C, D	IPR006680	Amidohydrolase-related	Domain
A, B, C, D	IPR032466	Metal-dependent hydrolase	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.