Structure of human VCP/p97 hexamer bound to ADP (DMSO control). Determined by electron microscopy at 2.3 Å resolution. Released 18 Mar 2026.
Explore 10QR in 3D Show helices and sheets RCSB PDB PDBe
10QR contains 240 α-helices and 156 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-29 | 3 | 1 |
| β-strand | 38-41 | 4 | 2 |
| β-strand | 57-59 | 3 | 3 |
| α-helix | 62-64 | 3 | |
| β-strand | 67-69 | 3 | 3 |
| β-strand | 70-73 | 4 | 2 |
| β-strand | 81-83 | 3 | 1 |
| α-helix | 86-92 | 7 | |
| β-strand | 102-104 | 3 | 3 |
| β-strand | 115-118 | 4 | 4 |
| α-helix | 131-134 | 4 | |
| α-helix | 136-139 | 4 | |
| β-strand | 145-147 | 3 | 5 |
| β-strand | 153-156 | 4 | 6 |
| β-strand | 159-162 | 4 | 6 |
| β-strand | 163-167 | 5 | 4 |
| β-strand | 173-175 | 3 | 5 |
| α-helix | 189-192 | 4 | |
| α-helix | 196-197 | 2 | |
| α-helix | 203-205 | 3 | |
| α-helix | 212-225 | 14 | |
| α-helix | 227-232 | 6 | |
| β-strand | 240-244 | 5 | 7 |
| α-helix | 251-262 | 12 | |
| β-strand | 265-268 | 4 | 7 |
| α-helix | 271-276 | 6 | |
| α-helix | 278 | 1 | |
| α-helix | 281-295 | 15 | |
| β-strand | 299-302 | 4 | 7 |
| α-helix | 306-309 | 4 | |
| α-helix | 319-325 | 7 | |
| α-helix | 328-334 | 7 | |
| β-strand | 341-347 | 7 | 7 |
| α-helix | 350-352 | 3 | |
| α-helix | 355-358 | 4 | |
| β-strand | 365-368 | 4 | 7 |
| α-helix | 374-384 | 11 | |
| α-helix | 398-401 | 4 | |
| α-helix | 408-424 | 17 | |
| α-helix | 439-444 | 6 | |
| α-helix | 449-457 | 9 | |
| β-strand | 470 | 1 | 8 |
| α-helix | 483-489 | 7 | |
| α-helix | 490-494 | 5 | |
| α-helix | 495-498 | 4 | |
| α-helix | 500-506 | 7 | |
| α-helix | 509-511 | 3 | |
| β-strand | 513-517 | 5 | 8 |
| α-helix | 524-535 | 12 | |
| β-strand | 538-542 | 5 | 8 |
| α-helix | 544-552 | 9 | |
| α-helix | 558-568 | 11 | |
| β-strand | 572-576 | 5 | 8 |
| α-helix | 581-585 | 5 | |
| α-helix | 599-610 | 12 | |
| β-strand | 617-623 | 7 | 8 |
| α-helix | 626-628 | 3 | |
| α-helix | 631-634 | 4 | |
| β-strand | 641-644 | 4 | 8 |
| α-helix | 650-661 | 12 | |
| β-strand | 666 | 1 | 9 |
| α-helix | 672-678 | 7 | |
| α-helix | 684-704 | 21 | |
| β-strand | 731 | 1 | 9 |
| α-helix | 733-740 | 8 | |
| α-helix | 749-764 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transitional endoplasmic reticulum ATPase | A, B, C, D, E, F | protein | 806 | Homo sapiens | P55072 (AlphaFold model) |
>10QR_1 Transitional endoplasmic reticulum ATPase (chains A, B, C, D, E, F) MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLK GKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPID DTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDT VIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRG ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF GRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAAL QAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIG GLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFI SIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRV INQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKAN LRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAM EVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGG AGPSQGSGGGTGGSVYTEDNDDDLYG
Development and Structural Characterization of UTE-156, a Covalent Inhibitor of the VCP/p97 AAA+ ATPase. Tamayo-Jaramillo, D., Hegde, S., Jia, X. et al. Adv Sci (Weinh) (2026) 13:e20545-e20545. DOI 10.1002/advs.202520545 · PubMed
Other PDB entries of the same protein (UniProt P55072 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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