1JK7
CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000070 | biological_process | mitotic sister chromatid segregation |
A | 0000165 | biological_process | MAPK cascade |
A | 0000775 | cellular_component | chromosome, centromeric region |
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 | 0005694 | cellular_component | chromosome |
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 | 0005856 | cellular_component | cytoskeleton |
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 | 0017018 | molecular_function | myosin 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 MN A 400 |
Chain | Residue |
A | ASP92 |
A | ASN124 |
A | HIS173 |
A | HIS248 |
A | MN401 |
A | HOH2118 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 401 |
Chain | Residue |
A | HIS248 |
A | MN400 |
A | HOH2118 |
A | ASP64 |
A | HIS66 |
A | ASP92 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 2022 |
Chain | Residue |
A | LYS211 |
A | PHE258 |
A | ALA259 |
A | LYS260 |
A | HOH2053 |
A | HOH2139 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE OKA A 501 |
Chain | Residue |
A | ARG96 |
A | HIS125 |
A | ILE130 |
A | TYR134 |
A | GLN181 |
A | ARG188 |
A | ASP220 |
A | ARG221 |
A | LYS234 |
A | HIS237 |
A | TYR272 |
A | CYS273 |
A | GLU275 |
A | PHE276 |
A | BME2025 |
A | HOH2119 |
A | HOH2120 |
A | HOH2131 |
A | HOH2132 |
A | HOH2133 |
A | HOH2134 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME A 2023 |
Chain | Residue |
A | TYR137 |
A | LYS141 |
A | ARG261 |
A | HOH2138 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME A 2024 |
Chain | Residue |
A | ILE169 |
A | LEU289 |
A | MET290 |
A | CYS291 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME A 2025 |
Chain | Residue |
A | ASP208 |
A | ARG221 |
A | GLN249 |
A | OKA501 |
A | HOH2123 |
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 | ACT_SITE: Proton donor => ECO:0000269|PubMed:7500362 |
Chain | Residue | Details |
A | HIS125 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11535607, ECO:0000269|PubMed:15280359 |
Chain | Residue | Details |
A | ASP64 | |
A | HIS66 | |
A | ASP92 | |
A | ASN124 | |
A | HIS173 | |
A | HIS248 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Inhibition by microcystin toxin binding |
Chain | Residue | Details |
A | CYS273 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | THR307 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR311 |
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 |