10QQ: Human VCP/p97 dodecamer

Structure of human VCP/p97 dodecamer bound to ADP (DMSO control). Determined by electron microscopy at 2.13 Å resolution. Released 18 Mar 2026.

Method: Electron microscopy
Resolution: 2.13 Å
Organism: Homo sapiens
Chains: 12
Atoms: 69,804
Mol. weight: 1084.08 kDa
Ligands: MG, ADP
Released: 18 Mar 2026

Explore 10QQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

10QQ contains 480 α-helices and 312 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.

Chains A, C, D, E, F, G, I, J, K and L: 40 helices, 26 β-strands

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	749-760	12

Chains B and H: 40 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	27-29	3	10
β-strand	38-41	4	11
β-strand	57-59	3	12
α-helix	62-64	3
β-strand	67-69	3	12
β-strand	70-73	4	11
β-strand	81-83	3	10
α-helix	86-92	7
β-strand	102-104	3	12
β-strand	115-118	4	13
α-helix	131-134	4
α-helix	136-139	4
β-strand	145-147	3	14
β-strand	153-156	4	15
β-strand	159-162	4	15
β-strand	163-167	5	13
β-strand	173-175	3	14
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	16
α-helix	251-262	12
β-strand	265-268	4	16
α-helix	271-276	6
α-helix	278	1
α-helix	281-295	15
β-strand	299-302	4	16
α-helix	306-309	4
α-helix	319-325	7
α-helix	328-334	7
β-strand	341-347	7	16
α-helix	350-352	3
α-helix	355-358	4
β-strand	365-368	4	16
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	17
α-helix	483-489	7
α-helix	490-494	5
α-helix	495-498	4
α-helix	500-505	6
α-helix	509-511	3
β-strand	513-517	5	17
α-helix	524-535	12
β-strand	538-542	5	17
α-helix	544-552	9
α-helix	558-568	11
β-strand	572-576	5	17
α-helix	581-585	5
α-helix	599-610	12
β-strand	617-623	7	17
α-helix	626-628	3
α-helix	631-634	4
β-strand	641-644	4	17
α-helix	650-661	12
β-strand	666	1	18
α-helix	672-678	7
α-helix	684-704	21
β-strand	731	1	18
α-helix	733-740	8
α-helix	749-760	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transitional endoplasmic reticulum ATPase	A, B, C, D, E, F, G, H, I, J, K, L	protein	806	Homo sapiens	P55072 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA

>10QQ_1 Transitional endoplasmic reticulum ATPase (chains A, B, C, D, E, F, G, H, I, J, K, L)
MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLK
GKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPID
DTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDT
VIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRG
ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI
IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF
GRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAAL
QAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIG
GLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFI
SIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRV
INQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKAN
LRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAM
EVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGG
AGPSQGSGGGTGGSVYTEDNDDDLYG

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	24
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	24

Primary citation

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:

5B6C 1.55 Å, Structural Details of Ufd1 binding to p97
7PUX 1.73 Å, Structure of p97 N-D1(L198W) in complex with Fragment TROLL2
3TIW 1.8 Å, Crystal structure of p97N in complex with the C-terminus of gp78
4KDL 1.81 Å, Crystal structure of p97/VCP N in complex with OTU1 UBXL
4KDI 1.86 Å, Crystal structure of p97/VCP N in complex with OTU1 UBXL
5EPP 1.88 Å, Structural Insights into the Interaction of p97 N-terminus Domain and VBM Motif in…
3EBB 1.9 Å, PLAP/P97 complex
6G2V 1.9 Å, Crystal structure of the p97 D2 domain in a helical split-washer conformation
6G2Z 1.92 Å, Crystal structure of the p97 D2 domain in a helical split-washer conformation
4KO8 1.98 Å, Structure of p97 N-D1 R155H mutant in complex with ATPgS
3QQ8 2.0 Å, Crystal structure of p97-N in complex with FAF1-UBX
3QWZ 2.0 Å, Crystal structure of FAF1 UBX-p97N-domain complex

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