Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8FVI

Human APOBEC3H bound to HIV-1 Vif in complex with CBF-beta, ELOB, ELOC, and CUL5

Functional Information from GO Data
ChainGOidnamespacecontents
00003713molecular_functiontranscription coactivator activity
00005634cellular_componentnucleus
10003723molecular_functionRNA binding
10005515molecular_functionprotein binding
10016020cellular_componentmembrane
10019058biological_processviral life cycle
10020002cellular_componenthost cell plasma membrane
10030430cellular_componenthost cell cytoplasm
10033644cellular_componenthost cell membrane
10044423cellular_componentvirion component
A0000932cellular_componentP-body
A0002376biological_processimmune system process
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0004126molecular_functioncytidine deaminase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0010526biological_processtransposable element silencing
A0016554biological_processcytidine to uridine editing
A0016787molecular_functionhydrolase activity
A0044355biological_processclearance of foreign intracellular DNA
A0044828biological_processnegative regulation by host of viral genome replication
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
A0046872molecular_functionmetal ion binding
A0051607biological_processdefense response to virus
A0070383biological_processDNA cytosine deamination
x0006511biological_processubiquitin-dependent protein catabolic process
x0031625molecular_functionubiquitin protein ligase binding
y0006368biological_processtranscription elongation by RNA polymerase II
y0030891cellular_componentVCB complex
y0070449cellular_componentelongin complex
z0006511biological_processubiquitin-dependent protein catabolic process
Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEicFIneiksmgldetqcyqvtcyltws..........PCss......CaweL
ChainResidueDetails
AHIS54-LEU92
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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_FI2
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_FI3
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_FI4
Number of Residues1
DetailsRegion: {"description":"Membrane association","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues31
DetailsMotif: {"description":"HCCH motif","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues9
DetailsMotif: {"description":"BC-box-like motif","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by host MAP4K1","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by host MAP4K1","evidences":[{"source":"HAMAP-Rule","id":"MF_04081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues122
DetailsDomain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"29290613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6B0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BBO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29290613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6B0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BBO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues65
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
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

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon