1K46

Crystal Structure of the Type III Secretory Domain of Yersinia YopH Reveals a Domain-Swapped Dimer

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	d1k46a_	Alpha and beta proteins (a+b)	YopH tyrosine phosphatase N-terminal domain	YopH tyrosine phosphatase N-terminal domain	YopH tyrosine phosphatase N-terminal domain	YopH tyrosine phosphatase N-terminal domain	(Yersinia pseudotuberculosis ) [TaxId: 633 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	YopH tyrosine phosphatase N-terminal domain	8025416	4003675	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	YopH tyrosine phosphatase N-terminal domain	8037795	3001250	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	YopH_N	e1k46A1	A: a+b complex topology	X: YopH tyrosine phosphatase N-terminal domain (From Topology)	H: YopH tyrosine phosphatase N-terminal domain (From Topology)	T: YopH tyrosine phosphatase N-terminal domain	F: YopH_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1570.10	Alpha Beta	2-Layer Sandwich	YopH tyrosine phosphatase N-terminal domain	Protein-tyrosine phosphatase, YopH, N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09013	YopH, N-terminal (YopH_N)	YopH, N-terminal	The N-terminal domain of YopH is a compact structure composed of four alpha-helices and two beta-hairpins. Helices alpha-1 and alpha-3 are parallel to each other and antiparallel to helices alpha-2 and alpha-4. This domain targets YopH for secretion ...	The N-terminal domain of YopH is a compact structure composed of four alpha-helices and two beta-hairpins. Helices alpha-1 and alpha-3 are parallel to each other and antiparallel to helices alpha-2 and alpha-4. This domain targets YopH for secretion from the bacterium and translocation into eukaryotic cells, and has phosphotyrosyl peptide-binding activity, allowing for recognition of p130Cas and paxillin [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN-TYROSINE PHOSPHATASE YOPH	phosphoric ester hydrolase activity phosphoprotein phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity phosphatase activity hydrolase activity catalytic activity	dephosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR003546	Type III secreted modular tyrosine phosphatase, SptP/YopH	Family
A	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A	IPR000387	Tyrosine-specific protein phosphatases domain	Domain
A	IPR036484	Protein-tyrosine phosphatase, YopH, N-terminal domain superfamily	Homologous Superfamily
A	IPR003595	Protein-tyrosine phosphatase, catalytic	Domain
A	IPR000242	Tyrosine-specific protein phosphatase, PTPase domain	Domain
A	IPR016130	Protein-tyrosine phosphatase, active site	Active Site
A	IPR015103	Protein-tyrosine phosphatase, YopH, N-terminal	Domain

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.