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9QSH

Cryo-EM structure of the MMM ubiquitin ligase complex with nanobody 992 (Composite map)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0031647biological_processregulation of protein stability
A0045664biological_processregulation of neuron differentiation
A0045879biological_processnegative regulation of smoothened signaling pathway
A0060170cellular_componentciliary membrane
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005769cellular_componentearly endosome
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006513biological_processprotein monoubiquitination
D0007224biological_processsmoothened signaling pathway
D0008333biological_processendosome to lysosome transport
D0016020cellular_componentmembrane
D0016567biological_processprotein ubiquitination
D0032100biological_processpositive regulation of appetite
D0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
D0045879biological_processnegative regulation of smoothened signaling pathway
D0048022biological_processnegative regulation of melanin biosynthetic process
D0061630molecular_functionubiquitin protein ligase activity
D0070062cellular_componentextracellular exosome
D0106072biological_processnegative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway
D0140311molecular_functionprotein sequestering activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues39
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues102
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

256158

PDB entries from 2026-07-08

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