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8VLB

Crystal structure of EloBC-VHL-CDO1 complex bound to compound 4 molecular glue

Functional Information from GO Data
ChainGOidnamespacecontents
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000151cellular_componentubiquitin ligase complex
B0001222molecular_functiontranscription corepressor binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006351biological_processDNA-templated transcription
B0006367biological_processtranscription initiation at RNA polymerase II promoter
B0006368biological_processtranscription elongation by RNA polymerase II
B0016567biological_processprotein ubiquitination
B0030891cellular_componentVCB complex
B0031462cellular_componentCul2-RING ubiquitin ligase complex
B0031466cellular_componentCul5-RING ubiquitin ligase complex
B0031625molecular_functionubiquitin protein ligase binding
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0065003biological_processprotein-containing complex assembly
B0070449cellular_componentelongin complex
B0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
B0140958biological_processtarget-directed miRNA degradation
B1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
B2000104biological_processnegative regulation of DNA-templated DNA replication
C0006511biological_processubiquitin-dependent protein catabolic process
D0000097biological_processsulfur amino acid biosynthetic process
D0005506molecular_functioniron ion binding
D0005829cellular_componentcytosol
D0006534biological_processcysteine metabolic process
D0006954biological_processinflammatory response
D0007595biological_processlactation
D0008198molecular_functionferrous iron binding
D0008270molecular_functionzinc ion binding
D0016151molecular_functionnickel cation binding
D0016491molecular_functionoxidoreductase activity
D0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D0017172molecular_functioncysteine dioxygenase activity
D0019448biological_processL-cysteine catabolic process
D0033762biological_processresponse to glucagon
D0042412biological_processtaurine biosynthetic process
D0043200biological_processresponse to amino acid
D0045471biological_processresponse to ethanol
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
D0051384biological_processresponse to glucocorticoid
D0051591biological_processresponse to cAMP
D0097184biological_processresponse to azide
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsRegion: {"description":"Involved in binding to CCT complex"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"Interaction with Elongin BC complex"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues65
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17135237","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"3'-(S-cysteinyl)-tyrosine (Cys-Tyr)","evidences":[{"source":"PubMed","id":"17135237","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-01-28

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