9Z06: Lymphoid-specific helicase
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state. Determined by electron microscopy at 3.39 Å resolution. Released 29 Apr 2026.
- Method
- Electron microscopy
- Resolution
- 3.39 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 15,531
- Mol. weight
- 583.31 kDa
- Released
- 29 Apr 2026
Explore 9Z06 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9Z06 contains 96 α-helices and 58 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: 16 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-27 | 3 | |
| α-helix | 28-57 | 30 | |
| α-helix | 59-99 | 41 | |
| α-helix | 225-238 | 14 | |
| β-strand | 244-248 | 5 | 1 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 1 |
| α-helix | 280-282 | 3 | |
| α-helix | 283-293 | 11 | |
| β-strand | 299-301 | 3 | 1 |
| α-helix | 306-316 | 11 | |
| β-strand | 320 | 1 | 2 |
| β-strand | 325 | 1 | 2 |
| β-strand | 328-331 | 4 | 1 |
| α-helix | 333-338 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 348 | 1 | 3 |
| β-strand | 350-354 | 5 | 1 |
| α-helix | 364-370 | 7 | |
| β-strand | 375 | 1 | 3 |
| β-strand | 378-382 | 5 | 1 |
| α-helix | 390-400 | 11 | |
| α-helix | 407-409 | 3 | |
| α-helix | 410-421 | 12 | |
| α-helix | 427-444 | 18 | |
| α-helix | 445-447 | 3 | |
| β-strand | 448-451 | 4 | 1 |
Chain B: 15 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-57 | 30 | |
| α-helix | 59-94 | 36 | |
| α-helix | 225-238 | 14 | |
| β-strand | 244-246 | 3 | 4 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 4 |
| α-helix | 280-282 | 3 | |
| α-helix | 283-293 | 11 | |
| β-strand | 299-301 | 3 | 4 |
| α-helix | 306-317 | 12 | |
| β-strand | 320 | 1 | 5 |
| β-strand | 325 | 1 | 5 |
| β-strand | 328-331 | 4 | 4 |
| α-helix | 333-338 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 348 | 1 | 6 |
| β-strand | 350-354 | 5 | 4 |
| α-helix | 365-370 | 6 | |
| β-strand | 375 | 1 | 6 |
| β-strand | 378-381 | 4 | 4 |
| α-helix | 390-400 | 11 | |
| α-helix | 402-404 | 3 | |
| α-helix | 410-419 | 10 | |
| α-helix | 427-444 | 18 | |
| α-helix | 445-447 | 3 | |
| β-strand | 448-449 | 2 | 4 |
Chain C: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-57 | 30 | |
| α-helix | 59-91 | 33 | |
| α-helix | 225-238 | 14 | |
| β-strand | 244-247 | 4 | 7 |
| α-helix | 255-266 | 12 | |
| β-strand | 274-278 | 5 | 7 |
| α-helix | 283-293 | 11 | |
| β-strand | 299-301 | 3 | 7 |
| α-helix | 306-317 | 12 | |
| β-strand | 320 | 1 | 8 |
| β-strand | 325 | 1 | 8 |
| α-helix | 326-327 | 2 | |
| β-strand | 328-332 | 5 | 7 |
| α-helix | 333-338 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 348-354 | 7 | 7 |
| α-helix | 364-370 | 7 | |
| β-strand | 375-382 | 8 | 7 |
| α-helix | 390-400 | 11 | |
| α-helix | 402-404 | 3 | |
| α-helix | 407-409 | 3 | |
| α-helix | 410-422 | 13 | |
| α-helix | 427-444 | 18 | |
| α-helix | 445-447 | 3 | |
| β-strand | 448-449 | 2 | 7 |
Chain D: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-57 | 30 | |
| α-helix | 59-100 | 42 | |
| α-helix | 225-238 | 14 | |
| β-strand | 244-246 | 3 | 9 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-278 | 5 | 9 |
| α-helix | 280-282 | 3 | |
| α-helix | 283-293 | 11 | |
| β-strand | 299-301 | 3 | 9 |
| α-helix | 306-317 | 12 | |
| β-strand | 320 | 1 | 10 |
| β-strand | 325 | 1 | 10 |
| α-helix | 326-327 | 2 | |
| β-strand | 328-332 | 5 | 9 |
| α-helix | 333-338 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 348-354 | 7 | 9 |
| α-helix | 365-370 | 6 | |
| β-strand | 375-381 | 7 | 9 |
| α-helix | 390-400 | 11 | |
| α-helix | 407-409 | 3 | |
| α-helix | 410-422 | 13 | |
| α-helix | 427-443 | 17 | |
| α-helix | 445-447 | 3 | |
| β-strand | 448-449 | 2 | 9 |
Chain E: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-57 | 30 | |
| α-helix | 59-96 | 38 | |
| α-helix | 225-238 | 14 | |
| β-strand | 244-246 | 3 | 11 |
| α-helix | 248-249 | 2 | |
| α-helix | 256-266 | 11 | |
| β-strand | 274-278 | 5 | 11 |
| α-helix | 280-282 | 3 | |
| α-helix | 283-293 | 11 | |
| β-strand | 299-301 | 3 | 11 |
| α-helix | 306-317 | 12 | |
| β-strand | 320 | 1 | 12 |
| β-strand | 325 | 1 | 12 |
| α-helix | 326-327 | 2 | |
| β-strand | 328-332 | 5 | 11 |
| α-helix | 333-338 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 350-354 | 5 | 11 |
| α-helix | 367-370 | 4 | |
| β-strand | 378-381 | 4 | 11 |
| α-helix | 390-400 | 11 | |
| α-helix | 402-404 | 3 | |
| α-helix | 407-409 | 3 | |
| α-helix | 410-422 | 13 | |
| α-helix | 427-444 | 18 | |
| α-helix | 445-447 | 3 | |
| β-strand | 448-449 | 2 | 11 |
Chain F: 15 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-57 | 30 | |
| α-helix | 59-95 | 37 | |
| α-helix | 225-238 | 14 | |
| β-strand | 244-246 | 3 | 13 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-278 | 5 | 13 |
| α-helix | 280-282 | 3 | |
| α-helix | 283-293 | 11 | |
| β-strand | 299-301 | 3 | 13 |
| α-helix | 306-317 | 12 | |
| β-strand | 320 | 1 | 14 |
| β-strand | 325 | 1 | 14 |
| α-helix | 326-327 | 2 | |
| β-strand | 328-332 | 5 | 13 |
| α-helix | 333-338 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 348-354 | 7 | 13 |
| α-helix | 364-370 | 7 | |
| β-strand | 375-381 | 7 | 13 |
| α-helix | 390-400 | 11 | |
| α-helix | 407-409 | 3 | |
| α-helix | 410-419 | 10 | |
| α-helix | 427-444 | 18 | |
| β-strand | 449 | 1 | 13 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Lymphoid-specific helicase | A, B, C, D, E, F | protein | 838 | Homo sapiens | Q9NRZ9 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>9Z06_1 Lymphoid-specific helicase (chains A, B, C, D, E, F)
MPAERPAGSGGSEAPAMVEQLDTAVITPAMLEEEEQLEAAGLERERKMLEKARMSWDRES
TEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLERKKESLKVKKGKNSIDASE
EKPVMRKKRGREDESYNISEVMSKEEILSVAKKNKKENEDENSSSTNLCVEDLQKNKDSN
SIIKDRLSETVRQNTKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWEN
GINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTM
LYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIK
NMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSL
SETAEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVALEVPPKREVVVYAPLSKKQEIFY
TAIVNRTIANMFGSSEKETIELSPTGRPKRRTRKSINYSKIDDFPNELEKLISQIQPEVD
RERAVVEVNIPVESEVNLKLQNIMMLLRKCCNHPYLIEYPIDPVTQEFKIDEELVTNSGK
FLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHS
FNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY
RLVTANTIDQKIVERAAAKRKLEKLIIHKNHFKGGQSGLNLSKNFLDPKELMELLKSRDY
EREIKGSREKVISDKDLELLLDRSDLIDQMNASGPIKEKMGIFKILENSEDSSPECLF
Primary citation
Structure of human lymphoid-specific helicase HELLS in its autoinhibited state. Kaur, G., Ren, R., Lee, J. et al. Nucleic Acids Res (2026) 54. DOI 10.1093/nar/gkag326 · PubMed
Other PDB entries of the same protein (UniProt Q9NRZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9Z05 2.86 Å, Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state (D3)
- 9Z04 2.99 Å, Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
- 8SKZ 3.5 Å, Cryo-EM structure of DDM1-HELLS chimera bound to the nucleosome
Browse structure collections
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