4UPH

Crystal Structure of Phosphonate Monoester Hydrolase of Agrobacterium radiobacter

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Phosphonate monoester hydrolases-like	8045402	4004457	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Alkaline phosphatase-like	8090532	3001353	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Arylsulfatase C-terminal domain-like	8090533	3002305	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Arylsulfatase C-terminal domain-like	8090533	3002305	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Alkaline phosphatase-like	8090532	3001353	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Alkaline phosphatase-like	8090532	3001353	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Arylsulfatase C-terminal domain-like	8090533	3002305	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Alkaline phosphatase-like	8090532	3001353	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Arylsulfatase C-terminal domain-like	8090533	3002305	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	PF00884	e4uphA1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: PF00884	ECOD (1.6)
B	PF00884	e4uphB1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: PF00884	ECOD (1.6)
C	PF00884	e4uphC1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: PF00884	ECOD (1.6)
D	PF00884	e4uphD1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: PF00884	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)
B	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)
C	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)
D	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00884	Sulfatase (Sulfatase)	Sulfatase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	SULFATASE (SULFURIC ESTER HYDROLASE) PROTEIN	hydrolase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR000917	Sulfatase, N-terminal	Domain
A, B, C, D	IPR017850	Alkaline-phosphatase-like, core domain superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	DDZ	Parent Component: ALA RESID: AA0492 PSI-MOD : L-3,3-dihydroxyoalanine (Cys) MOD:01444 , L-3,3-dihydroxyoalanine (Ser) MOD:01445 , L-3,3-dihydroxyoalanine MOD:01448

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 R01GM133198.