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5BX1

Crystal Structure of PRL-1 complex with compound analogy 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005819cellular_componentspindle
A0005886cellular_componentplasma membrane
A0006470biological_processprotein dephosphorylation
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0030335biological_processpositive regulation of cell migration
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue 4XA A 201
ChainResidue
ATYR14
ALYS15
AASN16
ALYS38
AMET124
APHE132
AARG159

site_idAC2
Number of Residues11
Detailsbinding site for residue SO4 A 202
ChainResidue
AALA106
AGLY107
ALEU108
AGLY109
AARG110
AALA111
APRO112
AARG137
AHOH307
ACYS104
AVAL105

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 203
ChainResidue
ALYS125
AARG153
AMET156
AARG157
APHE160
AHOH308
AHOH316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues35
DetailsRegion: {"description":"Interaction with ATF5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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