Annotations: 1WVI

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1wvia_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NagD-like	Putative phosphatase SMU.1415c	(Streptococcus mutans UA159 ) [TaxId: 210007 ],	SCOPe (2.08)
B	d1wvib_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NagD-like	Putative phosphatase SMU.1415c	(Streptococcus mutans UA159 ) [TaxId: 210007 ],	SCOPe (2.08)
C	d1wvic_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NagD-like	Putative phosphatase SMU.1415c	(Streptococcus mutans UA159 ) [TaxId: 210007 ],	SCOPe (2.08)
D	d1wvid_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NagD-like	Putative phosphatase SMU.1415c	(Streptococcus mutans UA159 ) [TaxId: 210007 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	NagD-like	8031353	4001039	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	HAD-like	8043731	3001890	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	HAD-like	8043731	3001890	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	HAD-like	8043731	3001890	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	HAD-like	8043731	3001890	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	F_UNCLASSIFIED	e1wviA3	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF13242,PF13344	e1wviA2	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: PF13242,PF13344	ECOD (1.6)
B	F_UNCLASSIFIED	e1wviB1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF13242,PF13344	e1wviB2	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: PF13242,PF13344	ECOD (1.6)
C	F_UNCLASSIFIED	e1wviC1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: F_UNCLASSIFIED	ECOD (1.6)
C	PF13242,PF13344	e1wviC2	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: PF13242,PF13344	ECOD (1.6)
D	F_UNCLASSIFIED	e1wviD2	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: F_UNCLASSIFIED	ECOD (1.6)
D	PF13242,PF13344	e1wviD1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: PF13242,PF13344	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
B	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
C	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
D	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF13242	HAD-hyrolase-like (Hydrolase_like)	HAD-hyrolase-like	-	Domain
A, B, C, D	PF13344	Haloacid dehalogenase-like hydrolase (Hydrolase_6)	Haloacid dehalogenase-like hydrolase	This family is part of the HAD superfamily.	Domain

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036412	HAD-like superfamily	Homologous Superfamily
A, B, C, D	IPR023214	HAD superfamily	Homologous Superfamily
A, B, C, D	IPR006354	HAD-superfamily hydrolase, subfamily IIA, hypothetical 1	Family
A, B, C, D	IPR006357	HAD-superfamily hydrolase, subfamily IIA	Family

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.