1INP | pdb_00001inp

CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION

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	d1inpa_	Multi-domain proteins (alpha and beta)	Carbohydrate phosphatase	Carbohydrate phosphatase	Inositol monophosphatase/fructose-1,6-bisphosphatase-like	Inositol polyphosphate 1-phosphatase	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Inositol monophosphatase/fructose-1, 6-bisphosphatase-like	8025106	4002766	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Carbohydrate phosphatase-like	8037485	3001721	SCOP2 (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	Inositol_P_N	e1inpA1	A: a+b two layers	X: a+b domain in carbohydrate phosphatases (From Topology)	H: a+b domain in carbohydrate phosphatases (From Topology)	T: a+b domain in carbohydrate phosphatases	F: Inositol_P_N	ECOD (1.6)
A	Inositol_P_C_1	e1inpA2	A: a/b three-layered sandwiches	X: Rossmann-like domain in carbohydrate phosphatases (From Homology)	H: Rossmann-like domain in carbohydrate phosphatases	T: Rossmann-like domain in carbohydrate phosphatases	F: Inositol_P_C_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	4.10.460.10	Few Secondary Structures	Irregular	Inositol Polyphosphate 1-phosphatase	domain 1	CATH (4.3.0)
A	3.30.540.10	Alpha Beta	2-Layer Sandwich	Fructose-1,6-Bisphosphatase	Chain A, domain 1	CATH (4.3.0)
A	3.40.190.80	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00459	Inositol monophosphatase family (Inositol_P)	Inositol monophosphatase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	INOSITOL POLYPHOSPHATE 1-PHOSPHATASE	inositol trisphosphate phosphatase activity phosphoric ester hydrolase activity inositol phosphate phosphatase activity hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity inositol-1,3,4-trisphosphate 1-phosphatase activity catalytic activity inositol-1,4-bisphosphate 1-phosphatase activity inositol bisphosphate phosphatase activity cation binding ion binding binding metal ion binding inositol trisphosphate phosphatase activity phosphoric ester hydrolase activity inositol phosphate phosphatase activity hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity inositol-1,3,4-trisphosphate 1-phosphatase activity catalytic activity inositol-1,4-bisphosphate 1-phosphatase activity inositol bisphosphate phosphatase activity cation binding ion binding binding metal ion binding small molecule binding	phosphatidylinositol metabolic process glycerophospholipid biosynthetic process glycerophospholipid metabolic process lipid biosynthetic process primary metabolic process phosphatidylinositol phosphate biosynthetic process phospholipid biosynthetic process phosphatidylinositol biosynthetic process phospholipid metabolic process biosynthetic process glycerolipid biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process phosphatidylinositol metabolic process glycerophospholipid biosynthetic process glycerophospholipid metabolic process lipid biosynthetic process primary metabolic process phosphatidylinositol phosphate biosynthetic process phospholipid biosynthetic process phosphatidylinositol biosynthetic process phospholipid metabolic process biosynthetic process glycerolipid biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process glycerolipid metabolic process phosphorus metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR020550	Inositol monophosphatase, conserved site	Conserved Site
A	IPR020583	Inositol monophosphatase, metal-binding site	Binding Site
A	IPR000760	Inositol monophosphatase-like	Family
A	IPR044897	Inositol polyphosphate 1-phosphatase, domain 1	Homologous Superfamily
A	IPR050725	CysQ/Inositol Monophosphatase	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	inositol-1,4-bisphosphate 1-phosphatase M-CSA #856	Inositol polyphosphate 1 -phosphatase (l-ptase) removes the l-position phosphate from inositol 1,4-bisphosphate, yielding inositol 4-phosphate. l-Ptase is a ubiquitous monomeric enzyme that requires Mg2+ for activity and is potently inhibited by Li+, leading to its use in therapeutic targets of lithium treatment for manic-depressive illnesses.	Defined by 7 residues: ASP:A-54GLU:A-79ASP:A-153ILE:A-155ASP:A-156THR:A-158ASP:A-317 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.3.57 (PDB Primary Data) Search M-CSA Motif + EC 3.1.3.57

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.