9KQO: RNF20/RNF40-RAD6A-Ub
cryo-EM structure of RNF20/RNF40-RAD6A-Ub in complex with H2BS112GlcNAc nucleosome. Determined by electron microscopy at 3.48 Å resolution. Released 31 Dec 2025.
- Method
- Electron microscopy
- Resolution
- 3.48 Å
- Organism
- Homo sapiens
- Chains
- 14
- Atoms
- 14,687
- Mol. weight
- 239.8 kDa
- Ligands
- NAG, ZN
- Released
- 31 Dec 2025
Explore 9KQO in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9KQO contains 49 α-helices and 46 β-strands across 12 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: 2 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 942-946 | 5 | |
| β-strand | 947 | 1 | 1 |
| β-strand | 955 | 1 | 1 |
| β-strand | 958-960 | 3 | 2 |
| β-strand | 966-967 | 2 | 2 |
| α-helix | 970-977 | 8 | |
| β-strand | 995-997 | 3 | 2 |
Chain B: 3 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 3 |
| β-strand | 12-16 | 5 | 3 |
| β-strand | 22 | 1 | 4 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 3 |
| β-strand | 48-49 | 2 | 3 |
| β-strand | 55 | 1 | 4 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-70 | 5 | 3 |
Chain C: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-21 | 5 | |
| α-helix | 27-36 | 10 | |
| β-strand | 42-43 | 2 | 5 |
| α-helix | 46-72 | 27 | |
| β-strand | 77-78 | 2 | 6 |
| α-helix | 80-88 | 9 | |
| α-helix | 91-96 | 6 | |
| β-strand | 100-102 | 3 | 7 |
Chain D: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-48 | 11 | |
| β-strand | 53-54 | 2 | 6 |
| α-helix | 56-83 | 28 | |
| β-strand | 88-89 | 2 | 5 |
| α-helix | 91-101 | 11 | |
| α-helix | 105-123 | 19 | |
Chain E: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 41-42 | 2 | |
| α-helix | 45-54 | 10 | |
| α-helix | 64-78 | 15 | |
| β-strand | 83-84 | 2 | 8 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 9 |
| α-helix | 121-130 | 10 | |
Chain F: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-41 | 11 | |
| β-strand | 45-46 | 2 | 9 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 8 |
| α-helix | 83-91 | 9 | |
| β-strand | 96-98 | 3 | 7 |
Chain G: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-21 | 5 | |
| α-helix | 27-36 | 10 | |
| β-strand | 42-43 | 2 | 10 |
| α-helix | 46-73 | 28 | |
| β-strand | 77-78 | 2 | 11 |
| α-helix | 80-89 | 10 | |
| α-helix | 91-96 | 6 | |
| β-strand | 101-102 | 2 | 12 |
Chain H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-48 | 11 | |
| β-strand | 53-54 | 2 | 11 |
| α-helix | 56-83 | 28 | |
| β-strand | 88-89 | 2 | 10 |
| α-helix | 91-101 | 11 | |
| α-helix | 104-123 | 20 | |
4 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 |
|---|
| E3 ubiquitin-protein ligase BRE1B | A | protein | 60 | Homo sapiens | O75150 (AlphaFold model) |
| Polyubiquitin-B | B | protein | 75 | Homo sapiens | J3QS39 (AlphaFold model) |
| Histone H2A type 1-B/E | C, G | protein | 129 | Homo sapiens | P04908 (AlphaFold model) |
| Histone H2B type 1-K | D, H | protein | 125 | Homo sapiens | O60814 (AlphaFold model) |
| Histone H3 | E, K | protein | 135 | Homo sapiens | A0A653DHJ5 |
| Histone H4 | F, L | protein | 102 | Homo sapiens | P62805 |
| DNA (147-mer) | I | DNA | 147 | Homo sapiens | |
| DNA (147-mer) | J | DNA | 147 | Homo sapiens | |
| E3 ubiquitin-protein ligase BRE1A | M | protein | 60 | Homo sapiens | Q5VTR2 |
| Ubiquitin-conjugating enzyme E2 A | R | protein | 150 | Homo sapiens | P49459 |
Sequence of entity 1 (A), FASTA
>9KQO_1 E3 ubiquitin-protein ligase BRE1B (chains A)
EYKARLTCPCCNTRKKDAVLTKCFHVFCFECVRGRYEARQRKCPKCNAAFGAHDFHRIYI
Sequence of entity 2 (B), FASTA
>9KQO_2 Polyubiquitin-B (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRG
Sequence of entity 3 (C, G), FASTA
>9KQO_3 Histone H2A type 1-B/E (chains C, G)
SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKT
ESHHKAKGK
Sequence of entity 4 (D, H), FASTA
>9KQO_4 Histone H2B type 1-K (chains D, H)
PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMG
IMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTC
YTSAK
Sequence of entity 5 (E, K), FASTA
>9KQO_5 Histone H3 (chains E, K)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLSAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 6 (F, L), FASTA
>9KQO_6 Histone H4 (chains F, L)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 7 (I), FASTA
>9KQO_7 DNA (147-MER) (chains I)
ACAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAA
AACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTG
AGCGGCCTCGGCACCGGGATTCTCCAG
Sequence of entity 8 (J), FASTA
>9KQO_8 DNA (147-MER) (chains J)
CTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAA
ACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA
GGCACGTGTCAGATATATACATCCTGT
Sequence of entity 9 (M), FASTA
>9KQO_9 E3 ubiquitin-protein ligase BRE1A (chains M)
DYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYI
Sequence of entity 10 (R), FASTA
>9KQO_10 Ubiquitin-conjugating enzyme E2 A (chains R)
MSTPARRRLMRDFKRLQEDPPAGVSGAPSENNIMVWNAVIFGPEGTPFEDGTFKLTIEFT
EEYPNKPPTVRFVSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWR
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| ZN | Zinc ion | Zn | 4 |
Primary citation
Allosteric activation of RNF20/RNF40-RAD6A-mediated H2BK120 monoubiquitylation by H2BS112 GlcNAcylation. Deng, Z., Tao, S., Du, Y. et al. Nat Chem Biol (2026) 22:740-750. DOI 10.1038/s41589-025-02109-6 · PubMed
Other PDB entries of the same protein (UniProt O75150 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8GUJ 2.8 Å, Bre1-nucleosome complex (Model II)
- 8GUI 2.81 Å, Bre1-nucleosome complex (Model I)
- 8IEJ 3.12 Å, RNF20-RNF40/hRad6A-Ub/nucleosome complex
Browse structure collections
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