Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XM2

Crystal structure of Human PRL-1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004725	molecular_function	protein tyrosine phosphatase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005819	cellular_component	spindle
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0006470	biological_process	protein dephosphorylation
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0016020	cellular_component	membrane
A	0016311	biological_process	dephosphorylation
A	0016787	molecular_function	hydrolase activity
A	0030335	biological_process	positive regulation of cell migration
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0004725	molecular_function	protein tyrosine phosphatase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005768	cellular_component	endosome
B	0005769	cellular_component	early endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005819	cellular_component	spindle
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0006470	biological_process	protein dephosphorylation
B	0009898	cellular_component	cytoplasmic side of plasma membrane
B	0016020	cellular_component	membrane
B	0016311	biological_process	dephosphorylation
B	0016787	molecular_function	hydrolase activity
B	0030335	biological_process	positive regulation of cell migration
C	0004721	molecular_function	phosphoprotein phosphatase activity
C	0004725	molecular_function	protein tyrosine phosphatase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005768	cellular_component	endosome
C	0005769	cellular_component	early endosome
C	0005783	cellular_component	endoplasmic reticulum
C	0005819	cellular_component	spindle
C	0005856	cellular_component	cytoskeleton
C	0005886	cellular_component	plasma membrane
C	0006470	biological_process	protein dephosphorylation
C	0009898	cellular_component	cytoplasmic side of plasma membrane
C	0016020	cellular_component	membrane
C	0016311	biological_process	dephosphorylation
C	0016787	molecular_function	hydrolase activity
C	0030335	biological_process	positive regulation of cell migration
D	0004721	molecular_function	phosphoprotein phosphatase activity
D	0004725	molecular_function	protein tyrosine phosphatase activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005768	cellular_component	endosome
D	0005769	cellular_component	early endosome
D	0005783	cellular_component	endoplasmic reticulum
D	0005819	cellular_component	spindle
D	0005856	cellular_component	cytoskeleton
D	0005886	cellular_component	plasma membrane
D	0006470	biological_process	protein dephosphorylation
D	0009898	cellular_component	cytoplasmic side of plasma membrane
D	0016020	cellular_component	membrane
D	0016311	biological_process	dephosphorylation
D	0016787	molecular_function	hydrolase activity
D	0030335	biological_process	positive regulation of cell migration
E	0004721	molecular_function	phosphoprotein phosphatase activity
E	0004725	molecular_function	protein tyrosine phosphatase activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005768	cellular_component	endosome
E	0005769	cellular_component	early endosome
E	0005783	cellular_component	endoplasmic reticulum
E	0005819	cellular_component	spindle
E	0005856	cellular_component	cytoskeleton
E	0005886	cellular_component	plasma membrane
E	0006470	biological_process	protein dephosphorylation
E	0009898	cellular_component	cytoplasmic side of plasma membrane
E	0016020	cellular_component	membrane
E	0016311	biological_process	dephosphorylation
E	0016787	molecular_function	hydrolase activity
E	0030335	biological_process	positive regulation of cell migration
F	0004721	molecular_function	phosphoprotein phosphatase activity
F	0004725	molecular_function	protein tyrosine phosphatase activity
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005768	cellular_component	endosome
F	0005769	cellular_component	early endosome
F	0005783	cellular_component	endoplasmic reticulum
F	0005819	cellular_component	spindle
F	0005856	cellular_component	cytoskeleton
F	0005886	cellular_component	plasma membrane
F	0006470	biological_process	protein dephosphorylation
F	0009898	cellular_component	cytoplasmic side of plasma membrane
F	0016020	cellular_component	membrane
F	0016311	biological_process	dephosphorylation
F	0016787	molecular_function	hydrolase activity
F	0030335	biological_process	positive regulation of cell migration

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 181

Chain	Residue
A	SER104
A	VAL105
A	ALA106
A	GLY107
A	LEU108
A	GLY109
A	ARG110
A	HOH206

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 182

Chain	Residue
B	SER104
B	VAL105
B	ALA106
B	GLY107
B	LEU108
B	GLY109
B	ARG110
B	ASP72

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 183

Chain	Residue
C	SER104
C	VAL105
C	ALA106
C	GLY107
C	LEU108
C	GLY109
C	ARG110

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 184

Chain	Residue
D	SER104
D	ALA106
D	GLY107
D	LEU108
D	GLY109
D	ARG110

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 185

Chain	Residue
E	SER104
E	VAL105
E	ALA106
E	LEU108
E	GLY109
E	ARG110

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 186

Chain	Residue
F	SER104
F	VAL105
F	ALA106
F	GLY107
F	LEU108
F	GLY109
F	ARG110

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor => ECO:0000305

Chain	Residue	Details
A	ASP72
B	ASP72
C	ASP72
D	ASP72
E	ASP72
F	ASP72

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Phosphocysteine intermediate => ECO:0000255\|PROSITE-ProRule:PRU00160

Chain	Residue	Details
A	SER104
B	SER104
C	SER104
D	SER104
E	SER104
F	SER104

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	VAL105
E	ARG110
F	VAL105
F	ARG110
A	ARG110
B	VAL105
B	ARG110
C	VAL105
C	ARG110
D	VAL105
D	ARG110
E	VAL105

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Cysteine methyl ester => ECO:0000305

Chain	Residue	Details
A	CYS170
B	CYS170
C	CYS170
D	CYS170
E	CYS170
F	CYS170

site_id	SWS_FT_FI5
Number of Residues	6
Details	LIPID: S-farnesyl cysteine => ECO:0000269\|PubMed:9018080

Chain	Residue	Details
A	CYS170
B	CYS170
C	CYS170
D	CYS170
E	CYS170
F	CYS170

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1d5r

Chain	Residue	Details
A	SER104
A	ARG110
A	ASP72

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1d5r

Chain	Residue	Details
B	SER104
B	ARG110
B	ASP72

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1d5r

Chain	Residue	Details
C	SER104
C	ARG110
C	ASP72

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1d5r

Chain	Residue	Details
D	SER104
D	ARG110
D	ASP72

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1d5r

Chain	Residue	Details
E	SER104
E	ARG110
E	ASP72

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1d5r

Chain	Residue	Details
F	SER104
F	ARG110
F	ASP72

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)