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1XWW

Crystal Structure of Human B-form Low Molecular Weight Phosphotyrosyl Phosphatase at 1.6 Angstrom Resolution

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
ACYS12
ALEU13
AGLY14
AASN15
AILE16
ACYS17
AARG18
AASP129

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
ATYR142
AARG150
AHOH221
AHOH319
AHOH322
ALEU29

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
ACYS12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
AARG18

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P11064
ChainResidueDetails
AASP129

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1939112
ChainResidueDetails
AALA1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:9038134
ChainResidueDetails
ATYR131
ATYR132

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 2024-09-11

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