5LXQ
Structure of PRL-1 in complex with the Bateman domain of CNNM2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0010960 | biological_process | magnesium ion homeostasis |
B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
B | 0004725 | molecular_function | protein tyrosine phosphatase activity |
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 | 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 | 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 | 0016020 | cellular_component | membrane |
C | 0016311 | biological_process | dephosphorylation |
C | 0016787 | molecular_function | hydrolase activity |
C | 0030335 | biological_process | positive regulation of cell migration |
H | 0010960 | biological_process | magnesium ion homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue ATP A 601 |
Chain | Residue |
A | THR451 |
A | ZN602 |
H | ATP601 |
H | ZN602 |
A | CYS456 |
A | PHE457 |
A | TYR478 |
A | THR479 |
A | ARG480 |
A | THR568 |
A | GLU570 |
A | ASP571 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue ZN A 602 |
Chain | Residue |
A | ATP601 |
H | ATP601 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue ATP H 601 |
Chain | Residue |
A | ATP601 |
A | ZN602 |
H | THR451 |
H | CYS456 |
H | PHE457 |
H | TYR478 |
H | THR479 |
H | ARG480 |
H | ILE566 |
H | THR568 |
H | GLU570 |
H | ASP571 |
H | ZN602 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue ZN H 602 |
Chain | Residue |
A | ATP601 |
H | ATP601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
B | ASP72 | |
C | ASP72 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160 |
Chain | Residue | Details |
B | CYS104 | |
C | CYS104 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | VAL105 | |
B | ARG110 | |
C | VAL105 | |
C | ARG110 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Cysteine methyl ester => ECO:0000305 |
Chain | Residue | Details |
B | CYS170 | |
C | CYS170 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | LIPID: S-farnesyl cysteine => ECO:0000269|PubMed:10747914 |
Chain | Residue | Details |
B | CYS170 | |
C | CYS170 |