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
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 19-20 | 2 | |
| α-helix | 23 | 1 | |
| β-strand | 29-36 | 8 | 1 |
| β-strand | 44-48 | 5 | 1 |
| β-strand | 50 | 1 | 2 |
| β-strand | 53 | 1 | 2 |
| α-helix | 55-65 | 11 | |
| β-strand | 74-79 | 6 | 1 |
| β-strand | 80-82 | 3 | 3 |
| α-helix | 83-85 | 3 | |
| α-helix | 86-98 | 13 | |
| β-strand | 102-105 | 4 | 1 |
| β-strand | 106 | 1 | 4 |
| β-strand | 108-110 | 3 | 3 |
| α-helix | 117-128 | 12 | |
| β-strand | 133 | 1 | 4 |
| α-helix | 138-146 | 9 | |
| α-helix | 154-155 | 2 | |
| α-helix | 159-181 | 23 | |
Chain E: 8 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| β-strand | 30-36 | 7 | 5 |
| α-helix | 40-42 | 3 | |
| β-strand | 45-46 | 2 | 5 |
| β-strand | 50 | 1 | 6 |
| β-strand | 53 | 1 | 6 |
| α-helix | 55-65 | 11 | |
| β-strand | 74-82 | 9 | 5 |
| α-helix | 83-85 | 3 | |
| α-helix | 86-98 | 13 | |
| β-strand | 102-110 | 9 | 5 |
| α-helix | 117-128 | 12 | |
| β-strand | 133-134 | 2 | 5 |
| α-helix | 138-148 | 11 | |
| α-helix | 159-181 | 23 | |
Chain o: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-14 | 7 | |
| α-helix | 16-23 | 8 | |
| β-strand | 27-28 | 2 | 7 |
| α-helix | 37-49 | 13 | |
| β-strand | 55 | 1 | 7 |
| β-strand | 58-59 | 2 | 7 |
| β-strand | 64-70 | 7 | 7 |
| β-strand | 86-87 | 2 | 7 |
| β-strand | 94-103 | 10 | 7 |
| β-strand | 106-115 | 10 | 7 |
| β-strand | 120-121 | 2 | 7 |
| β-strand | 124-127 | 4 | 7 |
| α-helix | 130-134 | 5 | |
| α-helix | 137-148 | 12 | |
Chain p: 10 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-13 | 9 | 7 |
| α-helix | 15-26 | 12 | |
| α-helix | 27-31 | 5 | |
| β-strand | 39-41 | 3 | 7 |
| β-strand | 51-59 | 9 | 7 |
| β-strand | 62-69 | 8 | 7 |
| β-strand | 83-91 | 9 | 7 |
| β-strand | 94-97 | 4 | 7 |
| α-helix | 100-111 | 12 | |
| α-helix | 119-125 | 7 | |
| α-helix | 127-129 | 3 | |
| α-helix | 136-138 | 3 | |
| α-helix | 145-153 | 9 | |
| α-helix | 155-157 | 3 | |
| α-helix | 162-164 | 3 | |
| α-helix | 166-169 | 4 | |
Chain s: 5 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-12 | 5 | |
| α-helix | 16-23 | 8 | |
| β-strand | 27-28 | 2 | 8 |
| α-helix | 37-49 | 13 | |
| β-strand | 56-58 | 3 | 8 |
| β-strand | 64-70 | 7 | 8 |
| β-strand | 85-87 | 3 | 8 |
| β-strand | 94-103 | 10 | 8 |
| β-strand | 106-115 | 10 | 8 |
| β-strand | 120-127 | 8 | 8 |
| α-helix | 130-134 | 5 | |
| α-helix | 137-146 | 10 | |
Chain t: 9 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-13 | 9 | 8 |
| α-helix | 15-26 | 12 | |
| α-helix | 27-31 | 5 | |
| β-strand | 39-41 | 3 | 8 |
| β-strand | 51-59 | 9 | 8 |
| β-strand | 62-70 | 9 | 8 |
| β-strand | 83-91 | 9 | 8 |
| β-strand | 94-97 | 4 | 8 |
| α-helix | 100-109 | 10 | |
| α-helix | 119-124 | 6 | |
| α-helix | 142-144 | 3 | |
| α-helix | 147-153 | 7 | |
| α-helix | 155-156 | 2 | |
| α-helix | 162-164 | 3 | |
| α-helix | 166-170 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| RNA (5'-r(p*up*gp*cp*cp*gp*gp*gp*up*a)-3') | C, G | RNA | 9 | Escherichia coli BL21(DE3) | |
| RNA (5'-r(*ap*up*ap*cp*cp*cp*gp*gp*cp*a)-3') | D, H | RNA | 10 | Escherichia coli BL21(DE3) | |
| single-stranded DNA cytosine deaminase | A, E | protein | 185 | Pan troglodytes | B7T0U6 (AlphaFold model) |
| Core-binding factor subunit beta | o, s | protein | 170 | Homo sapiens | Q13951 (AlphaFold model) |
| Virion infectivity factor | p, t | protein | 176 | Human immunodeficiency virus 1 | P12504 |
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
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 4 |
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:
- 5Z98 2.2 Å, Crystal Structure of the Primate APOBEC3H Dimer mediated by RNA Duplex
- 9E9V 4.0 Å, Structural Insights into HIV-1 Vif-Mediated Ubiquitination and Degradation of APOBEC3H
Browse structure collections
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