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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8CX0

Cryo-EM structure of human APOBEC3G/HIV-1 Vif/CBFbeta/ELOB/ELOC monomeric complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000932cellular_componentP-body
A0002230biological_processpositive regulation of defense response to virus by host
A0003723molecular_functionRNA binding
A0004126molecular_functioncytidine deaminase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008829molecular_functiondCTP deaminase activity
A0009972biological_processobsolete cytidine deamination
A0010526biological_processtransposable element silencing
A0016553biological_processbase conversion or substitution editing
A0016554biological_processcytidine to uridine editing
A0016787molecular_functionhydrolase activity
A0030895cellular_componentapolipoprotein B mRNA editing enzyme complex
A0042802molecular_functionidentical protein binding
A0045071biological_processnegative regulation of viral genome replication
A0045087biological_processinnate immune response
A0045869biological_processnegative regulation of single stranded viral RNA replication via double stranded DNA intermediate
A0048525biological_processnegative regulation of viral process
A0051607biological_processdefense response to virus
A0070383biological_processDNA cytosine deamination
A0140374biological_processantiviral innate immune response
A0140546biological_processdefense response to symbiont
A1990904cellular_componentribonucleoprotein complex
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0008289molecular_functionlipid binding
B0016020cellular_componentmembrane
B0019058biological_processviral life cycle
B0019079biological_processviral genome replication
B0020002cellular_componenthost cell plasma membrane
B0030430cellular_componenthost cell cytoplasm
B0030674molecular_functionprotein-macromolecule adaptor activity
B0039537biological_processsymbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway
B0042802molecular_functionidentical protein binding
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
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
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000151cellular_componentubiquitin ligase complex
D0001222molecular_functiontranscription corepressor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006367biological_processtranscription initiation at RNA polymerase II promoter
D0006368biological_processtranscription elongation by RNA polymerase II
D0016567biological_processprotein ubiquitination
D0030891cellular_componentVCB complex
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0031466cellular_componentCul5-RING ubiquitin ligase complex
D0031625molecular_functionubiquitin protein ligase binding
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0065003biological_processprotein-containing complex assembly
D0070449cellular_componentelongin complex
D0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
D0140958biological_processtarget-directed miRNA degradation
D1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
D2000104biological_processnegative regulation of DNA-templated DNA replication
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0000151cellular_componentubiquitin ligase complex
E0001222molecular_functiontranscription corepressor binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006357biological_processregulation of transcription by RNA polymerase II
E0006367biological_processtranscription initiation at RNA polymerase II promoter
E0006511biological_processubiquitin-dependent protein catabolic process
E0016567biological_processprotein ubiquitination
E0030674molecular_functionprotein-macromolecule adaptor activity
E0031462cellular_componentCul2-RING ubiquitin ligase complex
E0031466cellular_componentCul5-RING ubiquitin ligase complex
E0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
E0070449cellular_componentelongin complex
E0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
E0140958biological_processtarget-directed miRNA degradation
E1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
E2000104biological_processnegative regulation of DNA-templated DNA replication
Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAElcFLdvipfwkldldqdyrvtcftsws..........PCfs......CaqeM
ChainResidueDetails
AHIS257-MET295
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues109
DetailsDomain: {"description":"CMP/dCMP-type deaminase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues114
DetailsDomain: {"description":"CMP/dCMP-type deaminase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues127
DetailsRegion: {"description":"Necessary for homooligomerization"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues9
DetailsRegion: {"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18288108","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18849968","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19153609","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25542899","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ROV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ROW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37419875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8H0I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J62","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18288108","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18849968","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19153609","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25542899","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37419875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ROV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ROW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8H0I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J62","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKA","evidences":[{"source":"PubMed","id":"18836454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21659520","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKA and CAMK2","evidences":[{"source":"PubMed","id":"21659520","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues5
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23318957","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19887642","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23318957","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31253590","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23318957","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31253590","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19887642","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16636053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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