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5JNU

Crystal structure of mouse Low-Molecular Weight Protein Tyrosine Phosphatase type A (LMPTP-A) complexed with phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006470biological_processprotein dephosphorylation
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017124molecular_functionSH3 domain binding
A0042383cellular_componentsarcolemma
B0003993molecular_functionacid phosphatase activity
B0004721molecular_functionphosphoprotein phosphatase activity
B0004725molecular_functionprotein tyrosine phosphatase activity
B0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006470biological_processprotein dephosphorylation
B0009898cellular_componentcytoplasmic side of plasma membrane
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0017124molecular_functionSH3 domain binding
B0042383cellular_componentsarcolemma
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 B 201
ChainResidue
BCYS12
BLEU13
BGLY14
BASN15
BILE16
BCYS17
BARG18
BASP129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
ACYS12
BCYS12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
AARG18
BARG18

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
AASP129
BASP129

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
AALA1
BALA1

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P24666
ChainResidueDetails
ATYR131
ATYR132
BTYR131
BTYR132

218196

PDB entries from 2024-04-10

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