Structure of PDB 1xm2 Chain A Binding Site BS01

Receptor Information
>1xm2 Chain A (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 A Residue 181 [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 A106 G107 G109 R110
Binding residue
(residue number reindexed from 1)		S97 A99 G100 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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