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 | 0005886 | cellular_component | plasma membrane |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0009898 | cellular_component | cytoplasmic side of plasma 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 | 0005886 | cellular_component | plasma membrane |
| C | 0006470 | biological_process | protein dephosphorylation |
| C | 0009898 | cellular_component | cytoplasmic side of plasma 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 | 70 |
| Details | Region: {"description":"Interaction with ATF5","evidences":[{"source":"PubMed","id":"11278933","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 122 |
| Details | Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
