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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8SZK

The cryo-EM structure of PPP2R5A/HIV-1 Vif/CBFb/EloB/EloC complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000151cellular_componentubiquitin ligase complex
A0001222molecular_functiontranscription corepressor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006351biological_processDNA-templated transcription
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0006368biological_processtranscription elongation by RNA polymerase II
A0016567biological_processprotein ubiquitination
A0030891cellular_componentVCB complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031466cellular_componentCul5-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0065003biological_processprotein-containing complex assembly
A0070449cellular_componentelongin complex
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0140958biological_processtarget-directed miRNA degradation
A1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
A2000104biological_processnegative regulation of DNA-templated DNA replication
B0006511biological_processubiquitin-dependent protein catabolic process
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000209biological_processprotein polyubiquitination
C0003677molecular_functionDNA binding
C0003713molecular_functiontranscription coactivator activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0006357biological_processregulation of transcription by RNA polymerase II
C0006366biological_processtranscription by RNA polymerase II
C0016020cellular_componentmembrane
C0016513cellular_componentcore-binding factor complex
C0043371biological_processnegative regulation of CD4-positive, alpha-beta T cell differentiation
C0043378biological_processpositive regulation of CD8-positive, alpha-beta T cell differentiation
C0043565molecular_functionsequence-specific DNA binding
C0045893biological_processpositive regulation of DNA-templated transcription
D0000159cellular_componentprotein phosphatase type 2A complex
D0000775cellular_componentchromosome, centromeric region
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
D0019210molecular_functionkinase inhibitor activity
D0019888molecular_functionprotein phosphatase regulator activity
D0019900molecular_functionkinase binding
D0030018cellular_componentZ disc
D0031430cellular_componentM band
D0072542molecular_functionprotein phosphatase activator activity
D1903077biological_processnegative regulation of protein localization to plasma membrane
G0003723molecular_functionRNA binding
G0005515molecular_functionprotein binding
G0016020cellular_componentmembrane
G0019058biological_processviral life cycle
G0020002cellular_componenthost cell plasma membrane
G0030430cellular_componenthost cell cytoplasm
G0044423cellular_componentvirion component
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues65
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsRegion: {"description":"Interaction with host APOBEC3F; F1-box","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsRegion: {"description":"Interaction with host APOBEC3G; G-box","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues18
DetailsRegion: {"description":"Interaction with host APOBEC3F and APOBEC3G; FG-box","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues5
DetailsRegion: {"description":"Interaction with host APOBEC3F; F2-box","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues39
DetailsRegion: {"description":"RNA-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues13
DetailsRegion: {"description":"Multimerization","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsRegion: {"description":"Membrane association","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues31
DetailsMotif: {"description":"HCCH motif","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues9
DetailsMotif: {"description":"BC-box-like motif","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24402281","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37640699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4N9F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8FVI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Cleavage in virion (by viral protease)","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12186895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by host MAP4K1","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by host MAP4K1","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-28

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