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8J62

Cryo-EM structure of APOBEC3G-Vif complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
B0003824molecular_functioncatalytic activity
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
C0019058biological_processviral life cycle
D0003713molecular_functiontranscription coactivator activity
D0005634cellular_componentnucleus
E0019058biological_processviral life cycle
F0003713molecular_functiontranscription coactivator activity
F0005634cellular_componentnucleus
G0019058biological_processviral life cycle
H0003713molecular_functiontranscription coactivator activity
H0005634cellular_componentnucleus
I0019058biological_processviral life cycle
J0003713molecular_functiontranscription coactivator activity
J0005634cellular_componentnucleus
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
AHIS240-MET278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:24402281, ECO:0000269|PubMed:37640699, ECO:0007744|PDB:4N9F, ECO:0007744|PDB:8FVI
ChainResidueDetails
CHIS108
GGLU152
GGLU171
IHIS108
IGLU152
IGLU171
CGLU152
CGLU171
EHIS108
EGLU152
EGLU171
GHIS108

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage in virion (by viral protease) => ECO:0000255|HAMAP-Rule:MF_04081, ECO:0000269|PubMed:12186895
ChainResidueDetails
AGLU55
ACYS87
AASP90
BGLU55
BCYS87
BASP90

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by host MAP4K1 => ECO:0000255|HAMAP-Rule:MF_04081
ChainResidueDetails
CTHR96
ETHR96
GTHR96
ITHR96
BMET278
BPHE281

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by host => ECO:0000255|HAMAP-Rule:MF_04081
ChainResidueDetails
AGLY234
BGLY234

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine; by host MAP4K1 => ECO:0000255|HAMAP-Rule:MF_04081
ChainResidueDetails
ATHR21
BTHR21

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKA and CAMK2 => ECO:0000269|PubMed:21659520
ChainResidueDetails
AGLU208
BGLU208

site_idSWS_FT_FI7
Number of Residues10
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:23318957
ChainResidueDetails
AASP32
BTYR260
AHIS42
APHE140
AALA153
ATYR260
BASP32
BHIS42
BPHE140
BALA153

site_idSWS_FT_FI8
Number of Residues8
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:19887642, ECO:0000305|PubMed:23318957, ECO:0000305|PubMed:31253590
ChainResidueDetails
AHIS287
ALYS293
ASER324
BHIS287
BLYS293
BSER324

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:23318957, ECO:0000305|PubMed:31253590
ChainResidueDetails
AHIS53
AARG239
BHIS53
BARG239

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:19887642
ChainResidueDetails
ACYS291
BCYS291

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PDB entries from 2024-11-06

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