6OBP
Reconstituted PP1 holoenzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000164 | cellular_component | protein phosphatase type 1 complex |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0001111 | biological_process | RNA polymerase II promoter clearance |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0005912 | cellular_component | adherens junction |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0005979 | biological_process | regulation of glycogen biosynthetic process |
| A | 0005981 | biological_process | regulation of glycogen catabolic process |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0008157 | molecular_function | protein phosphatase 1 binding |
| A | 0010288 | biological_process | response to lead ion |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0032922 | biological_process | circadian regulation of gene expression |
| A | 0032968 | biological_process | positive regulation of transcription elongation by RNA polymerase II |
| A | 0034244 | biological_process | negative regulation of transcription elongation by RNA polymerase II |
| A | 0042587 | cellular_component | glycogen granule |
| A | 0042752 | biological_process | regulation of circadian rhythm |
| A | 0043021 | molecular_function | ribonucleoprotein complex binding |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0043153 | biological_process | entrainment of circadian clock by photoperiod |
| A | 0043197 | cellular_component | dendritic spine |
| A | 0043204 | cellular_component | perikaryon |
| A | 0043247 | biological_process | telomere maintenance in response to DNA damage |
| A | 0043558 | biological_process | regulation of translational initiation in response to stress |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0045725 | biological_process | positive regulation of glycogen biosynthetic process |
| A | 0046579 | biological_process | positive regulation of Ras protein signal transduction |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| A | 0050821 | biological_process | protein stabilization |
| A | 0051301 | biological_process | cell division |
| A | 0060828 | biological_process | regulation of canonical Wnt signaling pathway |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072357 | cellular_component | PTW/PP1 phosphatase complex |
| A | 0098609 | biological_process | cell-cell adhesion |
| A | 0098641 | molecular_function | cadherin binding involved in cell-cell adhesion |
| A | 0098793 | cellular_component | presynapse |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0180007 | molecular_function | RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity |
| A | 2000806 | biological_process | positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 401 |
| Chain | Residue |
| A | HIS66 |
| A | ASP92 |
| A | ASN124 |
| A | HIS125 |
| A | ARG221 |
| A | HIS248 |
| A | MN402 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 402 |
| Chain | Residue |
| A | HIS173 |
| A | HIS248 |
| A | PO4401 |
| A | ASP92 |
| A | ASN124 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | TYR114 |
| A | PRO115 |
| A | GLU116 |
| A | ASN117 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | LEU40 |
| A | ARG43 |
| A | GLU44 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | HIS239 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 C 401 |
| Chain | Residue |
| C | ARG155 |
| C | LYS175 |
| C | ARG197 |
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":"UniProtKB","id":"P36873","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30100357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35830882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35831509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36175670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39446389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SW5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 9"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 21 |
| Details | Repeat: {"description":"LRR 11"} |
| Chain | Residue | Details |
