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9E7K

Crystal structure of the UCH37 RPN13 DEUBAD complex bound to an inhibitory nanobody in the canonical ubiquitin binding site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000502cellular_componentproteasome complex
A0000723biological_processtelomere maintenance
A0003723molecular_functionRNA binding
A0004843molecular_functioncysteine-type deubiquitinase activity
A0004866molecular_functionendopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006275biological_processregulation of DNA replication
A0006281biological_processDNA repair
A0006282biological_processregulation of DNA repair
A0006310biological_processDNA recombination
A0006338biological_processchromatin remodeling
A0006508biological_processproteolysis
A0006974biological_processDNA damage response
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016579biological_processprotein deubiquitination
A0016787molecular_functionhydrolase activity
A0021670biological_processlateral ventricle development
A0030901biological_processmidbrain development
A0031011cellular_componentIno80 complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0033044biological_processregulation of chromosome organization
A0045739biological_processpositive regulation of DNA repair
A0045880biological_processpositive regulation of smoothened signaling pathway
A0045893biological_processpositive regulation of DNA-templated transcription
A0045995biological_processregulation of embryonic development
A0048853biological_processforebrain morphogenesis
A0051726biological_processregulation of cell cycle
A0060382biological_processregulation of DNA strand elongation
A0061136biological_processregulation of proteasomal protein catabolic process
A0070628molecular_functionproteasome binding
A1904507biological_processpositive regulation of telomere maintenance in response to DNA damage
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for enzyme activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUP7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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