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5PNT

CRYSTAL STRUCTURE OF A HUMAN LOW MOLECULAR WEIGHT PHOSPHOTYROSYL PHOSPHATASE. IMPLICATIONS FOR SUBSTRATE SPECIFICITY

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
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006470biological_processprotein dephosphorylation
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016791molecular_functionphosphatase activity
A0042383cellular_componentsarcolemma
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MES A 0
ChainResidue
ACYS12
AASP129
ATYR131
AHOH161
ALEU13
AGLY14
AASN15
AILE16
ACYS17
AARG18
AGLU50
AARG97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
ALEU13

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
ASER19

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
APRO130

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1939112
ChainResidueDetails
AGLU2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:9038134
ChainResidueDetails
ATYR132
AGLY133

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pnt
ChainResidueDetails
ACYS17
AARG18
AASP129
ACYS12

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PDB entries from 2024-05-01

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