2Q5E

Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2

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)
A	d2q5ea_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2q5eb_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2q5ec_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2q5ed_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d2q5ee_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d2q5ef_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d2q5eg_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d2q5eh_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	NLI interacting factor-like phosphatase	automated matches	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)
A	SCOP2 Family	NLI interacting factor-like phosphatase	8098107	4002095	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	HAD-like	8098108	3001890	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	HAD-like	8098108	3001890	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	HAD-like	8098108	3001890	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	HAD-like	8098108	3001890	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	HAD-like	8098108	3001890	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	HAD-like	8098108	3001890	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	HAD-like	8098108	3001890	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	HAD-like	8098108	3001890	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	NIF	e2q5eA1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
B	NIF	e2q5eB1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
C	NIF	e2q5eC1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
D	NIF	e2q5eD1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
E	NIF	e2q5eE1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
F	NIF	e2q5eF1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
G	NIF	e2q5eG1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)
H	NIF	e2q5eH1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: NIF	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
B	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
C	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
D	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
E	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
F	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
G	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
H	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	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	PF03031	NLI interacting factor-like phosphatase (NIF)	NLI interacting factor-like phosphatase	-	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	Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2	phosphoric ester hydrolase activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds myosin phosphatase activity phosphatase activity hydrolase activity catalytic activity RNA polymerase II CTD heptapeptide repeat modifying activity RNA polymerase II CTD heptapeptide repeat phosphatase activity cation binding ion binding binding phosphoric ester hydrolase activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds myosin phosphatase activity phosphatase activity hydrolase activity catalytic activity RNA polymerase II CTD heptapeptide repeat modifying activity RNA polymerase II CTD heptapeptide repeat phosphatase activity cation binding ion binding binding metal ion binding small molecule binding	regulation of cellular process regulation of protein modification process regulation of protein phosphorylation negative regulation of biological process negative regulation of phosphate metabolic process negative regulation of cellular metabolic process regulation of primary metabolic process organic substance metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process negative regulation of cellular process protein metabolic process protein modification process regulation of cellular process regulation of protein modification process regulation of protein phosphorylation negative regulation of biological process negative regulation of phosphate metabolic process negative regulation of cellular metabolic process regulation of primary metabolic process organic substance metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process negative regulation of cellular process protein metabolic process protein modification process phosphorus metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biological process organonitrogen compound metabolic process protein phosphorylation phosphorylation regulation of protein metabolic process cellular metabolic process negative regulation of metabolic process biological regulation primary metabolic process regulation of cellular metabolic process regulation of macromolecule metabolic process negative regulation of protein phosphorylation macromolecule modification negative regulation of phosphorus metabolic process metabolic process cellular process regulation of phosphorylation regulation of phosphorus metabolic process macromolecule metabolic process negative regulation of phosphorylation regulation of metabolic process regulation of cell cycle phase transition negative regulation of cell cycle cell cycle phase transition regulation of cell cycle G1/S phase transition cell cycle G1/S phase transition mitotic cell cycle negative regulation of mitotic cell cycle regulation of mitotic cell cycle negative regulation of cell cycle phase transition cell cycle regulation of cell cycle cell cycle process negative regulation of G1/S transition of mitotic cell cycle negative regulation of mitotic cell cycle phase transition regulation of cell cycle process negative regulation of cell cycle G1/S phase transition negative regulation of cell cycle process regulation of mitotic cell cycle phase transition mitotic cell cycle process regulation of G1/S transition of mitotic cell cycle G1/S transition of mitotic cell cycle mitotic cell cycle phase transition protein dephosphorylation dephosphorylation	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle 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	IPR004274	FCP1 homology domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR040078	CTD small RNA polymerase II polypeptide A phosphatase-like	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036412	HAD-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR023214	HAD superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR011948	Dullard phosphatase domain, eukaryotic	Domain

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: O14595	astrocytic tumor glioblastoma Pick disease atypical teratoid rhabdoid tumor malignant glioma progressive supranuclear palsy endogenous depression ovarian cancer tuberculosis

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.