28MO: UBA6-UbDha-UBE2Z trapped ternary complex

Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (singly loaded). Determined by electron microscopy at 3.01 Å resolution. Released 23 Sept 2026.

Method: Electron microscopy
Resolution: 3.01 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,580
Mol. weight: 166.41 kDa
Ligands: IHP, ATP
Released: 23 Sept 2026

Explore 28MO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

28MO contains 76 α-helices and 68 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.

Chain A: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	85-87	3
α-helix	89-92	4
α-helix	98-113	16
α-helix	115-116	2
β-strand	119-123	5	1
β-strand	130-136	7	1
α-helix	137-138	2
β-strand	147-153	7	1
β-strand	164-167	4	1
β-strand	178	1	2
β-strand	181	1	2
β-strand	186	1	1
β-strand	187	1	2
α-helix	190-192	3
α-helix	206-215	10
α-helix	221-224	4
α-helix	236-247	12
α-helix	248-255	8
α-helix	256-258	3
α-helix	265-288	24
α-helix	290-292	3
α-helix	295	1
β-strand	296	1	3
α-helix	297-298	2
β-strand	307	1	3
α-helix	310-329	20

Chain B: 58 helices, 51 β-strands

Element	Residues	Length	Sheet
α-helix	41-51	11
α-helix	53-59	7
β-strand	63-67	5	4
α-helix	71-83	13
β-strand	87-91	5	4
β-strand	95	1	5
α-helix	98-101	4
α-helix	109-114	6
β-strand	117	1	5
α-helix	120-127	8
β-strand	134-138	5	4
α-helix	148-153	6
β-strand	156-160	5	4
α-helix	164-174	11
α-helix	180-181	2
β-strand	182-189	8	4
β-strand	190	1	6
β-strand	192-198	7	4
β-strand	202-205	4	7
α-helix	211-213	3
β-strand	215-217	3	8
β-strand	218-222	5	9
β-strand	227-231	5	9
α-helix	232	1
β-strand	244-248	5	8
β-strand	251	1	10
α-helix	254-256	3
β-strand	257	1	8
β-strand	260-262	3	8
β-strand	264-267	4	9
β-strand	270-273	4	9
α-helix	280-282	3
β-strand	284	1	10
β-strand	287-291	5	8
β-strand	295-298	4	7
α-helix	302-305	4
β-strand	311	1	4
α-helix	312-313	2
α-helix	321-339	19
α-helix	342-344	3
α-helix	348-364	17
α-helix	373-381	9
β-strand	386	1	6
α-helix	388-407	20
α-helix	411-413	3
β-strand	416-417	2	4
β-strand	420	1	4
α-helix	422-426	5
α-helix	433-436	4
α-helix	444-459	16
β-strand	462-466	5	11
α-helix	470-482	13
β-strand	492-496	5	11
β-strand	500	1	12
α-helix	503-507	5
α-helix	514-516	3
β-strand	520	1	12
α-helix	521-532	12
β-strand	538-541	4	11
α-helix	547-549	3
α-helix	555-560	6
β-strand	563-566	4	11
α-helix	571-582	12
β-strand	588-594	7	11
β-strand	597-603	7	11
β-strand	608	1	13
α-helix	611-613	3
α-helix	616-620	5
α-helix	624-628	5
α-helix	634-646	13
α-helix	647-651	5
α-helix	652-662	11
α-helix	666-674	9
α-helix	682-690	9
α-helix	696-708	13
α-helix	709-713	5
α-helix	714-721	8
β-strand	727	1	14
β-strand	733	1	14
α-helix	752-768	17
α-helix	775-778	4
α-helix	780-787	8
α-helix	793-795	3
α-helix	819-833	15
α-helix	858-872	15
α-helix	880-888	9
α-helix	890-892	3
α-helix	895-914	20
α-helix	918-920	3
β-strand	922-927	6	11
β-strand	932-937	6	11
α-helix	938-939	2
β-strand	940	1	13
α-helix	941	1
β-strand	944-945	2	15
β-strand	951-952	2	15
β-strand	958-961	4	16
β-strand	967	1	17
α-helix	968-979	12
β-strand	983-988	6	18
β-strand	991-994	4	18
α-helix	1002-1006	5
β-strand	1008	1	17
α-helix	1009-1013	5
β-strand	1021-1024	4	16
β-strand	1025-1028	4	18
α-helix	1036-1037	2
β-strand	1038-1039	2	18
β-strand	1043-1046	4	16

Chain C: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	19
β-strand	12-16	5	19
β-strand	22	1	20
α-helix	23-33	11
β-strand	41-45	5	19
β-strand	48-49	2	19
β-strand	55	1	20
β-strand	66-71	6	19
α-helix	72-73	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 Z	A	protein	356	Homo sapiens	Q9H832 (AlphaFold model)
Ubiquitin-like modifier-activating enzyme 6	B	protein	1054	Homo sapiens	A0AVT1 (AlphaFold model)
Polyubiquitin-B	C	protein	76	Homo sapiens	P0CG47 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>28MO_1 Ubiquitin-conjugating enzyme E2 Z (chains A)
GPMAESPTEEAATAGAGAAGPGASSVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGP
GSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPG
MFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFN
PNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSK
NYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQ
DPFGEKRGHFDYQSLLMRLGLIRQKVLERLHNENAEMDSDSSSSGTETDLHGSLRV

Sequence of entity 2 (B), FASTA

>28MO_2 Ubiquitin-like modifier-activating enzyme 6 (chains B)
GPMEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQK
MAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNR
AEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQC
PPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHK
LETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVF
FESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLA
TSISETLEEKPDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLY
LEAADIVESLGKPECEEFLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKN
FALLGVGTSKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKI
DAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKG
HTEVIVPHLTESYNSHRDPPEEEIPFSTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNK
FWQTYSSAEEVLQKIQSGHSLEGCFQVIKLLSRRPRNWSQCVELARLKFEKYFNHKALQL
LHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPFAEEDL
SADALLNILSEVKIQEFKPSNKVVQTDETARKPDHVPISSEDERNAIFQLEKAILSNEAT
KSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTT
ATVSGLVALEMIKVTGGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRW
TVHGKEDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPGHAKRLKLTMHKLVKPTTE
KKYVDLTVSFAPDIDGDEDLPGPPVRYYFSHDTD

Sequence of entity 3 (C), FASTA

>28MO_3 Polyubiquitin-B (chains C)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGA

Ligands and cofactors

ID	Name	Formula	Copies
IHP	Inositol hexakisphosphate	C6 H18 O24 P6	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Primary citation

Structural determinants for FAT10 activation and transfer from UBA6 to E2 enzymes. Ellison, C.J., Riechmann, C., Dalietou, E.V. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-76603-3 · PubMed

Other PDB entries of the same protein (UniProt Q9H832 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5A4P 2.1 Å, Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation…
9YKV 2.73 Å, Cryo-EM structure of double-loaded human UBA6-UBE2Z-FAT10(t)/FAT10(a) thioester mimetic…
28MQ 3.04 Å, Cryo-EM structure of UBA6-FAT10Dha-UBE2Z trapped ternary complex
28MP 3.12 Å, Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (doubly loaded)
9YLF 3.14 Å, Cryo-EM structure of single-loaded human UBA6-UBE2Z/Ub(a) adenylate complex.
9YLB 3.24 Å, Cryo-EM structure of single-loaded human UBA6-UBE2Z/FAT10(a) adenylate complex.
9YKW 3.86 Å, Cryo-EM structure of double-loaded human UBA6-UBE2Z-Ub(t)/Ub(a) thioester mimetic complex.

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