5J16

Crystal structure of Inositol monophosphate bound SaIMPase-II

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	d5j16a_	Multi-domain proteins (alpha and beta)	Carbohydrate phosphatase	Carbohydrate phosphatase	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MSSA476 ) [TaxId: 282459 ],	SCOPe (2.08)
B	d5j16b1	Multi-domain proteins (alpha and beta)	Carbohydrate phosphatase	Carbohydrate phosphatase	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MSSA476 ) [TaxId: 282459 ],	SCOPe (2.08)
B	d5j16b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus subsp. aureus MSSA476 ) [TaxId: 282459 ],	SCOPe (2.08)
C	d5j16c_	Multi-domain proteins (alpha and beta)	Carbohydrate phosphatase	Carbohydrate phosphatase	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MSSA476 ) [TaxId: 282459 ],	SCOPe (2.08)
D	d5j16d_	Multi-domain proteins (alpha and beta)	Carbohydrate phosphatase	Carbohydrate phosphatase	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MSSA476 ) [TaxId: 282459 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Carbohydrate phosphatase-like	8079747	3001721	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Carbohydrate phosphatase-like	8079747	3001721	SCOP2B (2022-06-29)
C	SCOP2 Family	Inositol monophosphatase/fructose-1, 6-bisphosphatase-like	8079746	4002766	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Carbohydrate phosphatase-like	8079747	3001721	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Carbohydrate phosphatase-like	8079747	3001721	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	Inositol_P_N	e5j16A2	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	e5j16A1	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	ECOD (1.6)
B	Inositol_P_N	e5j16B2	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)
B	Inositol_P_C	e5j16B1	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	ECOD (1.6)
C	Inositol_P_N	e5j16C1	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)
C	Inositol_P_C	e5j16C2	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	ECOD (1.6)
D	Inositol_P_N	e5j16D1	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)
D	Inositol_P_C	e5j16D2	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	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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)
B	3.30.540.10	Alpha Beta	2-Layer Sandwich	Fructose-1,6-Bisphosphatase	Chain A, domain 1	CATH (4.3.0)
B	3.40.190.80	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.30.540.10	Alpha Beta	2-Layer Sandwich	Fructose-1,6-Bisphosphatase	Chain A, domain 1	CATH (4.3.0)
C	3.40.190.80	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D	3.30.540.10	Alpha Beta	2-Layer Sandwich	Fructose-1,6-Bisphosphatase	Chain A, domain 1	CATH (4.3.0)
D	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, B, C, D	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, B, C, D	Inositol monophosphatase family protein	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	IPR020583	Inositol monophosphatase, metal-binding site	Binding Site
A, B, C, D	IPR000760	Inositol monophosphatase-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.