1D1Q

CRYSTAL STRUCTURE OF A YEAST LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE (LTP1) COMPLEXED WITH THE SUBSTRATE PNPP

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	d1d1qa_	Alpha and beta proteins (a/b)	Phosphotyrosine protein phosphatases I-like	Phosphotyrosine protein phosphatases I	Low-molecular-weight phosphotyrosine protein phosphatases	Tyrosine phosphatase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
B	d1d1qb_	Alpha and beta proteins (a/b)	Phosphotyrosine protein phosphatases I-like	Phosphotyrosine protein phosphatases I	Low-molecular-weight phosphotyrosine protein phosphatases	Tyrosine phosphatase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Low-molecular-weight phosphotyrosine protein phosphatases	8031964	4000436	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphotyrosine protein phosphatases I	8044342	3000290	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Phosphotyrosine protein phosphatases I	8044342	3000290	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	LMWPc	e1d1qA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Phosphotyrosine protein phosphatases I-like	F: LMWPc	ECOD (1.6)
B	LMWPc	e1d1qB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Phosphotyrosine protein phosphatases I-like	F: LMWPc	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Response regulator	CATH (4.3.0)
B	3.40.50.2300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Response regulator	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01451	Low molecular weight phosphotyrosine protein phosphatase (LMWPc)	Low molecular weight phosphotyrosine protein phosphatase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	TYROSINE PHOSPHATASE (E.C.3.1.3.48)	phosphoric ester hydrolase activity acid phosphatase activity hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity catalytic activity phosphoprotein phosphatase activity catalytic activity, acting on a protein protein tyrosine phosphatase activity	protein dephosphorylation dephosphorylation primary metabolic process macromolecule modification phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process phosphorus metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR050438	Low Molecular Weight Phosphotyrosine Protein Phosphatase	Family
A, B	IPR017867	Protein-tyrosine phosphatase, low molecular weight	Family
A, B	IPR036196	Phosphotyrosine protein phosphatase I superfamily	Homologous Superfamily
A, B	IPR023485	Phosphotyrosine protein phosphatase I	Domain

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.