2BCD
X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000070 | biological_process | mitotic sister chromatid segregation |
| A | 0000165 | biological_process | MAPK cascade |
| A | 0000776 | cellular_component | kinetochore |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0001824 | biological_process | blastocyst development |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005521 | molecular_function | lamin binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0005815 | cellular_component | microtubule organizing center |
| A | 0005829 | cellular_component | cytosol |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0008157 | molecular_function | protein phosphatase 1 binding |
| A | 0016607 | cellular_component | nuclear speck |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0019903 | molecular_function | protein phosphatase binding |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0030182 | biological_process | neuron differentiation |
| A | 0030496 | cellular_component | midbody |
| A | 0032154 | cellular_component | cleavage furrow |
| A | 0032922 | biological_process | circadian regulation of gene expression |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042752 | biological_process | regulation of circadian rhythm |
| A | 0043153 | biological_process | entrainment of circadian clock by photoperiod |
| A | 0043197 | cellular_component | dendritic spine |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0046822 | biological_process | regulation of nucleocytoplasmic transport |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048511 | biological_process | rhythmic process |
| A | 0051301 | biological_process | cell division |
| A | 0060252 | biological_process | positive regulation of glial cell proliferation |
| A | 0072357 | cellular_component | PTW/PP1 phosphatase complex |
| A | 0098793 | cellular_component | presynapse |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 604 |
| Chain | Residue |
| A | ASN124 |
| A | GLU126 |
| A | CYS127 |
| A | SER129 |
| A | TRP206 |
| B | 1ZN3 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 605 |
| Chain | Residue |
| A | TRP206 |
| A | VAL195 |
| A | GLN198 |
| A | CYS202 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 400 |
| Chain | Residue |
| A | ASP92 |
| A | ASN124 |
| A | HIS173 |
| A | HIS248 |
| A | MN401 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | ASP64 |
| A | HIS66 |
| A | ASP92 |
| A | MN400 |
| A | HOH638 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ILE146 |
| A | LYS147 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 403 |
| Chain | Residue |
| A | SER22 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 404 |
| Chain | Residue |
| A | MET183 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN A 405 |
| Chain | Residue |
| A | ALA259 |
| A | LYS260 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR CHAIN B OF MOTUPORIN |
| Chain | Residue |
| A | ARG96 |
| A | SER129 |
| A | TYR134 |
| A | GLN185 |
| A | ARG188 |
| A | ASP220 |
| A | ARG221 |
| A | VAL223 |
| A | HIS237 |
| A | TYR272 |
| A | CYS273 |
| A | GLU275 |
| A | PHE276 |
| A | BME604 |
| A | HOH608 |
| A | HOH627 |
| A | HOH650 |
| A | HOH657 |
| A | HOH662 |
| A | HOH673 |
Functional Information from PROSITE/UniProt
| site_id | PS00125 |
| Number of Residues | 6 |
| Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
| Chain | Residue | Details |
| A | LEU121-GLU126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"7500362","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11535607","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15280359","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35768504","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SD0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Inhibition by microcystin toxin binding"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aui |
| Chain | Residue | Details |
| A | ASP95 | |
| A | HIS125 |
