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3EBQ

Crystal structure of human PPPDE1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006611biological_processprotein export from nucleus
A0008233molecular_functionpeptidase activity
A0008474molecular_functionpalmitoyl-(protein) hydrolase activity
A0016787molecular_functionhydrolase activity
A0016926biological_processprotein desumoylation
A0016929molecular_functiondeSUMOylase activity
A0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0052816molecular_functionlong-chain fatty acyl-CoA hydrolase activity
A0061676molecular_functionimportin-alpha family protein binding
A0098734biological_processmacromolecule depalmitoylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 201
ChainResidue
ACYS58
AGLY62

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 202
ChainResidue
AHIS38
ACYS108

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMotif: {"description":"Nuclear export signal 1","evidences":[{"source":"PubMed","id":"29666234","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01205","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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