1LJL

Wild Type pI258 S. aureus arsenate reductase

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ljla_	Alpha and beta proteins (a/b)	Phosphotyrosine protein phosphatases I-like	Phosphotyrosine protein phosphatases I	Low-molecular-weight phosphotyrosine protein phosphatases	Arsenate reductase ArsC	(Staphylococcus aureus ) [TaxId: 1280 ],	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	8028941	4000436	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphotyrosine protein phosphatases I	8041320	3000290	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	LMWPc	e1ljlA1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	arsenate reductase	arsenate reductase (thioredoxin) activity oxidoreductase activity arsenate reductase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding phosphoric ester hydrolase activity phosphoprotein phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity arsenate reductase (thioredoxin) activity oxidoreductase activity arsenate reductase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding 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	response to stimulus response to chemical response to arsenic-containing substance	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR014064	Arsenate reductase ArsC	Family
A	IPR036196	Phosphotyrosine protein phosphatase I superfamily	Homologous Superfamily
A	IPR023485	Phosphotyrosine protein phosphatase I	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	arsenate reductase M-CSA #143	Arsenate reductase (ArsC) from Staphylococcus aureus catalyses the reduction of arsenate to arsenite. It participates in the arsenic detoxification system of the gram-positive bacterium. ArsC also catalyses dephosphorylation in addition to reduction, although at a reduced efficiency. Arsenate reductase has a PTPase-I fold typical for low molecular weight tyrosine phosphatases which includes the catalytic P-loop and the similarity is corresponds to the similarity between arsenate and phosphate ions. The structural similarity of this fold has resulted in arsenate reductase displaying phosphatase activity in vitro as well as being able to reduce arsenate.	Defined by 14 residues: CYS:A-10THR:A-11GLY:A-12ASN:A-13SER:A-14CYS:A-15ARG:A-16SER:A-17SER:A-36THR:A-63ASP:A-65CYS:A-82CYS:A-89ASP:A-105 \| Explore in 3D: M-CSA Motif Definition Up to 10 residues are supported for Structure Motif searching, this motif has 14 residues. EC: 1.97.1.5 (PDB Primary Data)

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.