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9GSU

Structure of PP1-Neurabin bound to 4E-BP1.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005977biological_processglycogen metabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
D0004721molecular_functionphosphoprotein phosphatase activity
D0004722molecular_functionprotein serine/threonine phosphatase activity
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005977biological_processglycogen metabolic process
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
D0051301biological_processcell division
Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU121-GLU126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"O35867","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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