9E9V: Single-stranded DNA cytosine deaminase
Structural Insights into HIV-1 Vif-Mediated Ubiquitination and Degradation of APOBEC3H. Determined by electron microscopy at 4.0 Å resolution. Released 11 Mar 2026.
- Method
- Electron microscopy
- Resolution
- 4.0 Å
- Organisms
- Pan troglodytes, Escherichia coli BL21(DE3), Homo sapiens
- Chains
- 13
- Atoms
- 10,935
- Mol. weight
- 182.5 kDa
- Ligands
- ZN
- Released
- 11 Mar 2026
Explore 9E9V in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9E9V contains 57 α-helices and 69 β-strands across 9 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: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| β-strand | 30-36 | 7 | 1 |
| β-strand | 43 | 1 | 1 |
| β-strand | 46-47 | 2 | 1 |
| β-strand | 50 | 1 | 2 |
| β-strand | 53 | 1 | 2 |
| α-helix | 55-65 | 11 | |
| β-strand | 74-82 | 9 | 1 |
| α-helix | 83-85 | 3 | |
| α-helix | 86-98 | 13 | |
| β-strand | 103-105 | 3 | 1 |
| β-strand | 106 | 1 | 3 |
| β-strand | 108-110 | 3 | 1 |
| α-helix | 117-128 | 12 | |
| β-strand | 133 | 1 | 3 |
| α-helix | 138-147 | 10 | |
| α-helix | 159-169 | 11 | |
| α-helix | 174-181 | 8 | |
Chain B: 9 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 19-20 | 2 | |
| β-strand | 30-34 | 5 | 4 |
| α-helix | 40-42 | 3 | |
| β-strand | 43-47 | 5 | 4 |
| β-strand | 50 | 1 | 5 |
| β-strand | 53 | 1 | 5 |
| α-helix | 55-65 | 11 | |
| β-strand | 75-80 | 6 | 4 |
| α-helix | 83-85 | 3 | |
| α-helix | 86-98 | 13 | |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 106 | 1 | 6 |
| β-strand | 108 | 1 | 4 |
| α-helix | 117-128 | 12 | |
| β-strand | 133 | 1 | 6 |
| α-helix | 138-148 | 11 | |
| α-helix | 159-182 | 24 | |
Chain E: 10 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| β-strand | 30-31 | 2 | 7 |
| β-strand | 34-35 | 2 | 7 |
| α-helix | 41-43 | 3 | |
| β-strand | 46-47 | 2 | 7 |
| β-strand | 50 | 1 | 8 |
| β-strand | 53 | 1 | 8 |
| α-helix | 55-65 | 11 | |
| β-strand | 74-82 | 9 | 7 |
| α-helix | 83-85 | 3 | |
| α-helix | 86-98 | 13 | |
| β-strand | 102-110 | 9 | 7 |
| α-helix | 117-128 | 12 | |
| β-strand | 133-134 | 2 | 7 |
| α-helix | 138-142 | 5 | |
| α-helix | 143-148 | 6 | |
| α-helix | 154-155 | 2 | |
| α-helix | 160-181 | 22 | |
Chain m: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 9 |
| β-strand | 12-18 | 7 | 9 |
| α-helix | 24-34 | 11 | |
| β-strand | 44-46 | 3 | 10 |
| β-strand | 49-50 | 2 | 10 |
| α-helix | 51-52 | 2 | |
| α-helix | 58-60 | 3 | |
| β-strand | 73-75 | 3 | 9 |
| β-strand | 76-77 | 2 | 10 |
| α-helix | 91-94 | 4 | |
Chain n: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 9 |
| β-strand | 28-32 | 5 | 9 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 9 |
| α-helix | 67-83 | 17 | |
| α-helix | 97-110 | 14 | |
Chain o: 5 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-14 | 7 | |
| α-helix | 16-23 | 8 | |
| β-strand | 27 | 1 | 13 |
| α-helix | 37-49 | 13 | |
| β-strand | 55 | 1 | 11 |
| β-strand | 58 | 1 | 11 |
| β-strand | 59 | 1 | 13 |
| β-strand | 64-70 | 7 | 11 |
| β-strand | 85 | 1 | 14 |
| β-strand | 98 | 1 | 14 |
| β-strand | 99-103 | 5 | 12 |
| β-strand | 106-111 | 6 | 12 |
| β-strand | 124-127 | 4 | 12 |
| α-helix | 130-134 | 5 | |
| α-helix | 137-148 | 12 | |
Chain p: 9 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-13 | 9 | 11 |
| α-helix | 15-26 | 12 | |
| α-helix | 27-31 | 5 | |
| β-strand | 39-41 | 3 | 11 |
| β-strand | 51-59 | 9 | 11 |
| β-strand | 62-69 | 8 | 11 |
| β-strand | 83-91 | 9 | 11 |
| β-strand | 94-96 | 3 | 11 |
| β-strand | 97 | 1 | 12 |
| 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 | 162-164 | 3 | |
| α-helix | 166-169 | 4 | |
Chain s: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-12 | 5 | |
| α-helix | 16-23 | 8 | |
| β-strand | 28 | 1 | 17 |
| α-helix | 37-49 | 13 | |
| β-strand | 56 | 1 | 15 |
| β-strand | 58 | 1 | 17 |
| β-strand | 64-70 | 7 | 15 |
| β-strand | 86-91 | 6 | 16 |
| β-strand | 94-98 | 5 | 16 |
| β-strand | 101-103 | 3 | 16 |
| β-strand | 106-114 | 9 | 16 |
| β-strand | 123-127 | 5 | 16 |
| α-helix | 130-134 | 5 | |
| α-helix | 137-145 | 9 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| single-stranded DNA cytosine deaminase | A, B, E | protein | 183 | Pan troglodytes | B7T0U6 (AlphaFold model) |
| RNA (5'-r(p*cp*cp*cp*gp*gp*cp*a)-3') | D, H | RNA | 10 | Escherichia coli BL21(DE3) | |
| RNA (5'-r(p*gp*cp*cp*gp*gp*g)-3') | C, G | RNA | 9 | Escherichia coli BL21(DE3) | |
| Elongin-C | n | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| Elongin-B | m | protein | 102 | Homo sapiens | Q15370 (AlphaFold model) |
| Virion infectivity factor | p, t | protein | 176 | Human immunodeficiency virus 1 | P12504 |
| Core-binding factor subunit beta | o, s | protein | 170 | Homo sapiens | Q13951 |
Sequence of entity 1 (A, B, E), FASTA
>9E9V_1 single-stranded DNA cytosine deaminase (chains A, B, E)
MALLTAETFRLQFNNRRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFI
NEIKSMGLDETQCYQVTCYLTWSPCSSCAWKLVDFIQAHDHLNLRIFASRLYYHWCKPQQ
EGLRLLCGSQVPVEVMGLPEFNDCWENFVDHEKPLSFDPCKMLEELDKNSRAIKRRLERI
KQS
Sequence of entity 2 (D, H), FASTA
>9E9V_2 RNA (5'-R(P*CP*CP*CP*GP*GP*CP*A)-3') (chains D, H)
AUACCCGGCA
Sequence of entity 3 (C, G), FASTA
>9E9V_3 RNA (5'-R(P*GP*CP*CP*GP*GP*G)-3') (chains C, G)
UGCCGGGUA
Sequence of entity 4 (n), FASTA
>9E9V_4 Elongin-C (chains n)
MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY
FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 5 (m), FASTA
>9E9V_5 Elongin-B (chains m)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDV
Sequence of entity 6 (p, t), FASTA
>9E9V_6 Virion infectivity factor (chains p, t)
MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLG
DAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAI
RNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNK
Sequence of entity 7 (o, s), FASTA
>9E9V_7 Core-binding factor subunit beta (chains o, s)
MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVAT
GTNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLQRLD
GMGCLEFDEERAQQEDALAQQAFEEARRRTREFEDRDRSHREEMEVRVSQ
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
- 9E93 3.58 Å, Structural Insights into HIV-1 Vif-Mediated Ubiquitination and Degradation of APOBEC3H
Browse structure collections
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