2HV7

Crystal structure of phosphotyrosyl phosphatase activator bound to ATPgammaS

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2hv7b_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d2hv7g_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d2hv7h_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2hv7a_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2hv7c_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2hv7d_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d2hv7e_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d2hv7f_	All alpha proteins	PTPA-like	PTPA-like	PTPA-like	Serine/threonine-protein phosphatase 2A regulatory subunit B', PTPA	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	PTPA-like	8042445	3001997	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	PTPA-like	8042445	3001997	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)
B	PF03095	e2hv7B1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
G	PF03095	e2hv7G1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
H	PF03095	e2hv7H1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
A	PF03095	e2hv7A1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
C	PF03095	e2hv7C1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
D	PF03095	e2hv7D1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
E	PF03095	e2hv7E1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)
F	PF03095	e2hv7F1	A: alpha arrays	X: PTPA-like (From Topology)	H: PTPA-like (From Topology)	T: PTPA-like	F: PF03095	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
G	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
H	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
A	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
C	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
D	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
E	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)
F	1.20.120.1150	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Phosphotyrosyl phosphate activator, C-terminal lid domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF03095	Phosphotyrosyl phosphate activator (PTPA) protein (PTPA)	Phosphotyrosyl phosphate activator (PTPA) protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Protein phosphatase 2A, regulatory subunit B	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding protein binding signaling receptor binding isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity protein phosphatase binding phosphatase binding enzyme binding protein phosphatase 2A binding identical protein binding protein homodimerization activity protein dimerization activity enzyme regulator activity phosphatase regulator activity molecular function regulator activity protein phosphatase regulator activity protein phosphatase activator activity enzyme activator activity protein tyrosine phosphatase activator activity phosphatase activator activity molecular function activator activity	protein dephosphorylation regulation of cellular process regulation of phosphatase activity regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity negative regulation of cellular metabolic process regulation of primary metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process negative regulation of dephosphorylation phosphorus metabolic process protein modification process protein dephosphorylation regulation of cellular process regulation of phosphatase activity regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity negative regulation of cellular metabolic process regulation of primary metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process negative regulation of dephosphorylation phosphorus metabolic process protein modification process negative regulation of protein metabolic process regulation of biological process regulation of dephosphorylation cellular metabolic process negative regulation of metabolic process dephosphorylation regulation of protein metabolic process regulation of cellular metabolic process primary metabolic process regulation of molecular function regulation of hydrolase activity macromolecule modification regulation of phosphorus metabolic process metabolic process macromolecule metabolic process regulation of metabolic process negative regulation of hydrolase activity negative regulation of phosphoprotein phosphatase activity negative regulation of protein dephosphorylation regulation of protein modification process negative regulation of phosphate metabolic process regulation of phosphoprotein phosphatase activity organic substance metabolic process negative regulation of phosphatase activity negative regulation of cellular process protein metabolic process negative regulation of macromolecule metabolic process organonitrogen compound metabolic process regulation of protein dephosphorylation biological regulation negative regulation of molecular function regulation of macromolecule metabolic process negative regulation of phosphorus metabolic process cellular process positive regulation of phosphoprotein phosphatase activity positive regulation of phosphate metabolic process positive regulation of metabolic process positive regulation of phosphatase activity positive regulation of macromolecule metabolic process positive regulation of phosphorus metabolic process positive regulation of dephosphorylation positive regulation of protein metabolic process positive regulation of biological process positive regulation of cellular metabolic process positive regulation of molecular function positive regulation of protein modification process positive regulation of cellular process positive regulation of catalytic activity positive regulation of protein dephosphorylation positive regulation of hydrolase activity microtubule cytoskeleton organization mitotic cell cycle mitotic spindle organization cellular component organization organelle organization mitotic cell cycle process microtubule-based process cell cycle cellular component organization or biogenesis cytoskeleton organization microtubule cytoskeleton organization involved in mitosis spindle organization cell cycle process positive regulation of programmed cell death regulation of apoptotic process regulation of programmed cell death cell death positive regulation of apoptotic process apoptotic process programmed cell death	ATPase complex protein-containing complex catalytic complex phosphatase complex protein phosphatase type 2A complex protein serine/threonine phosphatase complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity ATPase complex protein-containing complex catalytic complex phosphatase complex protein phosphatase type 2A complex protein serine/threonine phosphatase complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm transmembrane transporter complex membrane membrane protein complex cation channel complex transporter complex calcium channel complex monoatomic ion channel complex nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR004327	Phosphotyrosyl phosphatase activator, PTPA	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR043170	Phosphotyrosyl phosphatase activator, C-terminal lid domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR037218	PTPA superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H	Pharos: Q15257	bipolar disorder gastric cancer major affective disorder 2 medulloblastoma Disease Exacerbation gastric neoplasm malignant ependymoma sleep-wake disorder hereditary diffuse gastric adenocarcinoma

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.