Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3RZ2

Crystal of Prl-1 complexed with peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005819cellular_componentspindle
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006470biological_processprotein dephosphorylation
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016311biological_processdephosphorylation
A0030335biological_processpositive regulation of cell migration
B0004721molecular_functionphosphoprotein phosphatase activity
B0004725molecular_functionprotein tyrosine phosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005819cellular_componentspindle
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006470biological_processprotein dephosphorylation
B0009898cellular_componentcytoplasmic side of plasma membrane
B0016311biological_processdephosphorylation
B0030335biological_processpositive regulation of cell migration
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR CHAIN C OF PRL-1 (PTP4A1)
ChainResidue
AARG47
AASP67
ATRP68
ALYS89
AILE90
AARG93
AARG153
AARG157
AARG159
BSER86
BARG157
ATYR53
BARG159
AASP54
ATHR55
ATHR56
AGLU59
AHIS64
AVAL65
ALEU66

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR CHAIN D OF PRL-1 (PTP4A1)
ChainResidue
BASP54
BTHR55
BTHR56
BTRP68
BASP83
DHOH20
DHOH36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP72
BASP72

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160
ChainResidueDetails
ACYS104
BCYS104

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL105
AARG110
BVAL105
BARG110

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon