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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyPhosphotyrosine protein phosphatases I 8044340 3000290 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ALMWPce1pntA1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: Phosphotyrosine protein phosphatases I-likeF: LMWPcECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.2300 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Response regulatorCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01451Low molecular weight phosphotyrosine protein phosphatase (LMWPc)Low molecular weight phosphotyrosine protein phosphatase- Domain

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

ChainsEnzyme NameDescriptionCatalytic Residues
low molecular weight phosphotyrosine protein phosphatase  M-CSA #462

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.

It is part of the PTPase superfamily. Has high homology to the Saccharomyces cerevisiae protein. Has conserved catalytic components, in particular the CXXXXXRS/T 'P loop'. The mechanism is therefore thought to be the same as that of the rest of the superfamily.

Defined by 6 residues: CYS:A-12ASN:A-15CYS:A-17ARG:A-18SER:A-19ASP:A-129
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