7MOG

Crystal Structure of Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1(AtPFA-DSP1 ) Cys150Ser in complex with 5-PCF2 Am-InsP5, an analogue of 5-InsP7

External Resource: Annotation

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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8044139	3000304	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8044139	3000304	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	DSPc	e7mogA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
B	DSPc	e7mogB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03162	Tyrosine phosphatase family (Y_phosphatase2)	Tyrosine phosphatase family	This family is closely related to the Pfam:PF00102 and Pfam:PF00782 families.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Tyrosine-protein phosphatase DSP1	phosphoric ester hydrolase activity phosphoprotein phosphatase activity non-membrane spanning protein tyrosine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity phosphatase activity hydrolase activity catalytic activity histone modifying activity histone phosphatase activity histone H2AXY142 phosphatase activity pyrophosphatase activity inositol bisdiphosphate tetrakisphosphate diphosphatase activity phosphoric ester hydrolase activity phosphoprotein phosphatase activity non-membrane spanning protein tyrosine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity phosphatase activity hydrolase activity catalytic activity histone modifying activity histone phosphatase activity histone H2AXY142 phosphatase activity pyrophosphatase activity inositol bisdiphosphate tetrakisphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides diphosphoinositol-polyphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity inositol diphosphate pentakisphosphate diphosphatase activity inositol diphosphate tetrakisphosphate diphosphatase activity inositol-5-diphosphate-1,3,4,6-tetrakisphosphate diphosphatase activity inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity protein tyrosine phosphatase activity, metal-dependent	-	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A, B	IPR020422	Dual specificity protein phosphatase domain	Domain
A, B	IPR020428	Atypical dual-specificity phosphatase Siw14-like, plant and fungi	Family
A, B	IPR016130	Protein-tyrosine phosphatase, active site	Active Site
A, B	IPR004861	Atypical dual-specificity phosphatase Siw14-like	Family

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.