9E93: Single-stranded DNA cytosine deaminase

Structural Insights into HIV-1 Vif-Mediated Ubiquitination and Degradation of APOBEC3H. Determined by electron microscopy at 3.58 Å resolution. Released 11 Mar 2026.

Method
Electron microscopy
Resolution
3.58 Å
Organisms
Escherichia coli BL21(DE3), Pan troglodytes, Homo sapiens
Chains
10
Atoms
8,773
Mol. weight
138.69 kDa
Ligands
ZN
Released
11 Mar 2026

Explore 9E93 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9E93 contains 47 α-helices and 45 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix6-127
α-helix19-202
α-helix231
β-strand29-3681
β-strand44-4851
β-strand5012
β-strand5312
α-helix55-6511
β-strand74-7961
β-strand80-8233
α-helix83-853
α-helix86-9813
β-strand102-10541
β-strand10614
β-strand108-11033
α-helix117-12812
β-strand13314
α-helix138-1469
α-helix154-1552
α-helix159-18123
Chain E: 8 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix6-127
β-strand30-3675
α-helix40-423
β-strand45-4625
β-strand5016
β-strand5316
α-helix55-6511
β-strand74-8295
α-helix83-853
α-helix86-9813
β-strand102-11095
α-helix117-12812
β-strand133-13425
α-helix138-14811
α-helix159-18123
Chain o: 5 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix8-147
α-helix16-238
β-strand27-2827
α-helix37-4913
β-strand5517
β-strand58-5927
β-strand64-7077
β-strand86-8727
β-strand94-103107
β-strand106-115107
β-strand120-12127
β-strand124-12747
α-helix130-1345
α-helix137-14812
Chain p: 10 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand5-1397
α-helix15-2612
α-helix27-315
β-strand39-4137
β-strand51-5997
β-strand62-6987
β-strand83-9197
β-strand94-9747
α-helix100-11112
α-helix119-1257
α-helix127-1293
α-helix136-1383
α-helix145-1539
α-helix155-1573
α-helix162-1643
α-helix166-1694
Chain s: 5 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix8-125
α-helix16-238
β-strand27-2828
α-helix37-4913
β-strand56-5838
β-strand64-7078
β-strand85-8738
β-strand94-103108
β-strand106-115108
β-strand120-12788
α-helix130-1345
α-helix137-14610
Chain t: 9 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand5-1398
α-helix15-2612
α-helix27-315
β-strand39-4138
β-strand51-5998
β-strand62-7098
β-strand83-9198
β-strand94-9748
α-helix100-10910
α-helix119-1246
α-helix142-1443
α-helix147-1537
α-helix155-1562
α-helix162-1643
α-helix166-1705

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RNA (5'-r(p*up*gp*cp*cp*gp*gp*gp*up*a)-3')C, GRNA9Escherichia coli BL21(DE3)
RNA (5'-r(*ap*up*ap*cp*cp*cp*gp*gp*cp*a)-3')D, HRNA10Escherichia coli BL21(DE3)
single-stranded DNA cytosine deaminaseA, Eprotein185Pan troglodytesB7T0U6 (AlphaFold model)
Core-binding factor subunit betao, sprotein170Homo sapiensQ13951 (AlphaFold model)
Virion infectivity factorp, tprotein176Human immunodeficiency virus 1P12504
Sequence of entity 1 (C, G), FASTA
>9E93_1 RNA (5'-R(P*UP*GP*CP*CP*GP*GP*GP*UP*A)-3') (chains C, G)
UGCCGGGUA
Sequence of entity 2 (D, H), FASTA
>9E93_2 RNA (5'-R(*AP*UP*AP*CP*CP*CP*GP*GP*CP*A)-3') (chains D, H)
AUACCCGGCA
Sequence of entity 3 (A, E), FASTA
>9E93_3 single-stranded DNA cytosine deaminase (chains A, E)
GSMALLTAETFRLQFNNRRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEIC
FINEIKSMGLDETQCYQVTCYLTWSPCSSCAWKLVDFIQAHDHLNLRIFASRLYYHWCKP
QQEGLRLLCGSQVPVEVMGLPEFNDCWENFVDHEKPLSFDPCKMLEELDKNSRAIKRRLE
RIKQS
Sequence of entity 4 (o, s), FASTA
>9E93_4 Core-binding factor subunit beta (chains o, s)
MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVAT
GTNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLQRLD
GMGCLEFDEERAQQEDALAQQAFEEARRRTREFEDRDRSHREEMEVRVSQ
Sequence of entity 5 (p, t), FASTA
>9E93_5 Virion infectivity factor (chains p, t)
MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLG
DAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAI
RNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

HIV-1 vif mediates ubiquitination of the proximal protomer in the APOBEC3H dimer to induce degradation. Skorupka, K.A., Matsuoka, K., Hassan, B. et al. Nat Commun (2025) 16:5879-5879. DOI 10.1038/s41467-025-60984-y · PubMed

Other PDB entries of the same protein (UniProt B7T0U6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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