ARP6-ZNHIT1 module from fully-engaged state of SRCAP-nucleosome complex, with H3-bound ARP6 (focused refinement, filtered by local resolution). Determined by electron microscopy at 3.2 Å resolution. Released 22 Jul 2026.
Explore 9PGD in 3D Show helices and sheets RCSB PDB PDBe
9PGD contains 29 α-helices and 27 β-strands across 3 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 1 |
| β-strand | 12-17 | 6 | 1 |
| β-strand | 23-26 | 4 | 1 |
| β-strand | 29-31 | 3 | 2 |
| β-strand | 40-41 | 2 | 2 |
| α-helix | 42-46 | 5 | |
| β-strand | 55-57 | 3 | 2 |
| β-strand | 60-61 | 2 | 3 |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 68-79 | 12 | |
| α-helix | 88-90 | 3 | |
| β-strand | 91-97 | 7 | 1 |
| α-helix | 103-111 | 9 | |
| α-helix | 112-116 | 5 | |
| β-strand | 121-126 | 6 | 1 |
| α-helix | 127-138 | 12 | |
| β-strand | 144-150 | 7 | 4 |
| β-strand | 155-161 | 7 | 4 |
| β-strand | 165 | 1 | 4 |
| β-strand | 171-173 | 3 | 4 |
| α-helix | 177-191 | 15 | |
| β-strand | 193 | 1 | 5 |
| α-helix | 199-209 | 11 | |
| α-helix | 216-224 | 9 | |
| β-strand | 234-237 | 4 | 6 |
| β-strand | 248-249 | 2 | 6 |
| α-helix | 250-251 | 2 | |
| α-helix | 252-254 | 3 | |
| β-strand | 267-270 | 4 | 6 |
| α-helix | 273-276 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 284-286 | 3 | |
| α-helix | 294-304 | 11 | |
| α-helix | 310-314 | 5 | |
| β-strand | 317-320 | 4 | 4 |
| α-helix | 322-325 | 4 | |
| α-helix | 329-340 | 12 | |
| β-strand | 349-350 | 2 | 4 |
| α-helix | 358-368 | 11 | |
| α-helix | 372-375 | 4 | |
| β-strand | 377-378 | 2 | 1 |
| α-helix | 379-381 | 3 | |
| α-helix | 382-386 | 5 | |
| α-helix | 387-393 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-34 | 14 | |
| α-helix | 84-91 | 8 | |
| β-strand | 105 | 1 | 4 |
| α-helix | 112-115 | 4 | |
| β-strand | 116 | 1 | 7 |
| β-strand | 123 | 1 | 7 |
| β-strand | 126-127 | 2 | 8 |
| β-strand | 134-135 | 2 | 8 |
| α-helix | 138-147 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-42 | 2 | |
| β-strand | 43 | 1 | 5 |
| α-helix | 45-53 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin-related protein 6 | C | protein | 396 | Homo sapiens | Q9GZN1 (AlphaFold model) |
| Zinc finger HIT domain-containing protein 1 | D | protein | 154 | Homo sapiens | O43257 (AlphaFold model) |
| Histone H3.2 | U | protein | 135 | Xenopus laevis | P84233 (AlphaFold model) |
>9PGD_1 Actin-related protein 6 (chains C) MTTLVLDNGAYNAKIGYSHENVSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPF QKGYLVNWDVQRQVWDYLFGKEMYQVDFLDTNIIITEPYFNFTSIQESMNEILFEEYQFQ AVLRVNAGALSAHRYFRDNPSELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLL TNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYRDMDIAKLKGEENTVMIDYVLPD FSTIKKGFCKPREEMVLSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVY SIQNLPEEMQPHFFKNIVLTGGNSLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYAW EGGKLISENDDFEDMVVTREDYEENGHSVCEEKFDI
>9PGD_2 Zinc finger HIT domain-containing protein 1 (chains D) MVEKKTSVRSQDPGQRRVLDRAARQRRINRQLEALENDNFQDDPHAGLPQLGKRLPQFDD DADTGKKKKKTRGDHFKLRFRKNFQALLEEQNLSVAEGPNYLTACAGPPSRPQRPFCAVC GFPSPYTCVSCGARYCTVRCLGTHQETRCLKWTV
>9PGD_3 Histone H3.2 (chains U) ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM PKDIQLARRIRGERA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
| MG | Magnesium ion | Mg | 1 |
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 1 |
Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme. Park, G., Wu, C., Louder, R.K. Sci Adv (2026) 12:eaei7728-eaei7728. DOI 10.1126/sciadv.aei7728 · PubMed
Other PDB entries of the same protein (UniProt Q9GZN1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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