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1XM2

Crystal structure of Human PRL-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005819cellular_componentspindle
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006338biological_processchromatin remodeling
A0006470biological_processprotein dephosphorylation
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016311biological_processdephosphorylation
A0030335biological_processpositive regulation of cell migration
A0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
A0140793molecular_functionhistone H2AXY142 phosphatase activity
B0004721molecular_functionphosphoprotein phosphatase activity
B0004725molecular_functionprotein tyrosine phosphatase activity
B0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005819cellular_componentspindle
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006338biological_processchromatin remodeling
B0006470biological_processprotein dephosphorylation
B0009898cellular_componentcytoplasmic side of plasma membrane
B0016311biological_processdephosphorylation
B0030335biological_processpositive regulation of cell migration
B0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
B0140793molecular_functionhistone H2AXY142 phosphatase activity
C0004721molecular_functionphosphoprotein phosphatase activity
C0004725molecular_functionprotein tyrosine phosphatase activity
C0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005768cellular_componentendosome
C0005769cellular_componentearly endosome
C0005783cellular_componentendoplasmic reticulum
C0005819cellular_componentspindle
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0006338biological_processchromatin remodeling
C0006470biological_processprotein dephosphorylation
C0009898cellular_componentcytoplasmic side of plasma membrane
C0016311biological_processdephosphorylation
C0030335biological_processpositive regulation of cell migration
C0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
C0140793molecular_functionhistone H2AXY142 phosphatase activity
D0004721molecular_functionphosphoprotein phosphatase activity
D0004725molecular_functionprotein tyrosine phosphatase activity
D0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005768cellular_componentendosome
D0005769cellular_componentearly endosome
D0005783cellular_componentendoplasmic reticulum
D0005819cellular_componentspindle
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0006338biological_processchromatin remodeling
D0006470biological_processprotein dephosphorylation
D0009898cellular_componentcytoplasmic side of plasma membrane
D0016311biological_processdephosphorylation
D0030335biological_processpositive regulation of cell migration
D0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
D0140793molecular_functionhistone H2AXY142 phosphatase activity
E0004721molecular_functionphosphoprotein phosphatase activity
E0004725molecular_functionprotein tyrosine phosphatase activity
E0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005768cellular_componentendosome
E0005769cellular_componentearly endosome
E0005783cellular_componentendoplasmic reticulum
E0005819cellular_componentspindle
E0005856cellular_componentcytoskeleton
E0005886cellular_componentplasma membrane
E0006338biological_processchromatin remodeling
E0006470biological_processprotein dephosphorylation
E0009898cellular_componentcytoplasmic side of plasma membrane
E0016311biological_processdephosphorylation
E0030335biological_processpositive regulation of cell migration
E0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
E0140793molecular_functionhistone H2AXY142 phosphatase activity
F0004721molecular_functionphosphoprotein phosphatase activity
F0004725molecular_functionprotein tyrosine phosphatase activity
F0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005768cellular_componentendosome
F0005769cellular_componentearly endosome
F0005783cellular_componentendoplasmic reticulum
F0005819cellular_componentspindle
F0005856cellular_componentcytoskeleton
F0005886cellular_componentplasma membrane
F0006338biological_processchromatin remodeling
F0006470biological_processprotein dephosphorylation
F0009898cellular_componentcytoplasmic side of plasma membrane
F0016311biological_processdephosphorylation
F0030335biological_processpositive regulation of cell migration
F0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
F0140793molecular_functionhistone H2AXY142 phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 181
ChainResidue
ASER104
AVAL105
AALA106
AGLY107
ALEU108
AGLY109
AARG110
AHOH206

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 182
ChainResidue
BSER104
BVAL105
BALA106
BGLY107
BLEU108
BGLY109
BARG110
BASP72

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 183
ChainResidue
CSER104
CVAL105
CALA106
CGLY107
CLEU108
CGLY109
CARG110

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 184
ChainResidue
DSER104
DALA106
DGLY107
DLEU108
DGLY109
DARG110

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E 185
ChainResidue
ESER104
EVAL105
EALA106
ELEU108
EGLY109
EARG110

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 F 186
ChainResidue
FSER104
FVAL105
FALA106
FGLY107
FLEU108
FGLY109
FARG110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AASP72
BASP72
CASP72
DASP72
EASP72
FASP72

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160
ChainResidueDetails
ASER104
BSER104
CSER104
DSER104
ESER104
FSER104

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AVAL105
EARG110
FVAL105
FARG110
AARG110
BVAL105
BARG110
CVAL105
CARG110
DVAL105
DARG110
EVAL105

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Cysteine methyl ester => ECO:0000305
ChainResidueDetails
ACYS170
BCYS170
CCYS170
DCYS170
ECYS170
FCYS170

site_idSWS_FT_FI5
Number of Residues6
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:9018080
ChainResidueDetails
ACYS170
BCYS170
CCYS170
DCYS170
ECYS170
FCYS170

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
ASER104
AARG110
AASP72

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
BSER104
BARG110
BASP72

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
CSER104
CARG110
CASP72

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
DSER104
DARG110
DASP72

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
ESER104
EARG110
EASP72

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
FSER104
FARG110
FASP72

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PDB entries from 2024-11-06

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