Structure of PDB 1xm2 Chain E Binding Site BS01

Receptor Information
>1xm2 Chain E (length=149) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTL
VEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHSVAG
LGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKM
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain1xm2 Chain E Residue 185 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xm2 Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms
Resolution2.7 Å
Binding residue
(original residue number in PDB)		S104 G109 R110
Binding residue
(residue number reindexed from 1)		S97 G102 R103
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.48: protein-tyrosine-phosphatase.
Gene Ontology
Molecular Function
GO:0004721 phosphoprotein phosphatase activity
GO:0004725 protein tyrosine phosphatase activity
GO:0005515 protein binding
Biological Process
GO:0006470 protein dephosphorylation
GO:0016311 dephosphorylation
GO:0030335 positive regulation of cell migration
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005768 endosome
GO:0005769 early endosome
GO:0005783 endoplasmic reticulum
GO:0005819 spindle
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0009898 cytoplasmic side of plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1xm2, PDBe:1xm2, PDBj:1xm2
PDBsum1xm2
PubMed15571731
UniProtQ93096|TP4A1_HUMAN Protein tyrosine phosphatase type IVA 1 (Gene Name=PTP4A1)

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