28MJ: UBA6

Cryo-EM structure of UBA6 in complex with FAT10 in the pre-adenylation state. Determined by electron microscopy at 2.77 Å resolution. Released 23 Sept 2026.

Method: Electron microscopy
Resolution: 2.77 Å
Organism: Homo sapiens
Chains: 2
Atoms: 9,334
Mol. weight: 138.09 kDa
Ligands: MG, ATP, IHP
Released: 23 Sept 2026

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

Secondary structure: helices and β-sheets

28MJ contains 67 α-helices and 62 β-strands across 2 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: 61 helices, 48 β-strands

Element	Residues	Length	Sheet
α-helix	41-51	11
α-helix	53-59	7
β-strand	63-67	5	5
α-helix	71-83	13
β-strand	87-91	5	5
α-helix	94	1
β-strand	95	1	6
α-helix	96	1
α-helix	98-102	5
α-helix	109-114	6
β-strand	117	1	6
α-helix	118-121	4
α-helix	123-127	5
β-strand	134-138	5	5
α-helix	149-153	5
β-strand	156-160	5	5
α-helix	164-175	12
α-helix	180-181	2
β-strand	182-189	8	5
β-strand	190	1	7
β-strand	192-198	7	5
β-strand	202-203	2	8
α-helix	213-214	2
β-strand	215-217	3	9
β-strand	218-222	5	10
β-strand	227-231	5	10
α-helix	232	1
β-strand	244-251	8	9
β-strand	257	1	9
β-strand	260-262	3	9
β-strand	263-267	5	10
β-strand	270-273	4	10
β-strand	284-291	8	9
β-strand	297-298	2	8
α-helix	302-305	4
α-helix	321-339	19
α-helix	342-344	3
α-helix	348-363	16
α-helix	369-371	3
α-helix	373-381	9
β-strand	386	1	7
α-helix	388-407	20
α-helix	411-413	3
β-strand	416-417	2	5
β-strand	420	1	5
α-helix	422-426	5
α-helix	433-435	3
α-helix	444-450	7
α-helix	452-459	8
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	547-550	4
α-helix	555-560	6
β-strand	563-566	4	11
α-helix	571-584	14
β-strand	588-594	7	11
β-strand	597-603	7	11
β-strand	608	1	13
α-helix	616-619	4
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	682-691	10
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	752-769	18
α-helix	775-778	4
α-helix	780-789	10
α-helix	792-795	4
α-helix	813-815	3
α-helix	818-833	16
α-helix	840-842	3
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	923-927	5	11
β-strand	932-936	5	11
α-helix	937-939	3
β-strand	940	1	13
α-helix	941	1
β-strand	944-947	4	15
β-strand	950-952	3	15
β-strand	958-961	4	16
β-strand	967	1	17
α-helix	968-979	12
β-strand	985-988	4	18
β-strand	991-994	4	18
α-helix	1000-1006	7
β-strand	1008	1	17
α-helix	1009-1012	4
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 B: 6 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	8-13	6	1
β-strand	20-24	5	1
β-strand	29	1	2
α-helix	30-40	11
β-strand	48-52	5	1
β-strand	55-56	2	1
β-strand	62	1	2
α-helix	64-66	3
β-strand	73-80	8	1
α-helix	82-84	3
β-strand	88-93	6	3
β-strand	101-106	6	3
β-strand	111	1	4
α-helix	112-123	12
α-helix	127-129	3
β-strand	132-134	3	3
β-strand	137-138	2	3
β-strand	144	1	4
α-helix	145-148	4
β-strand	155-158	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin D	B	protein	167	Homo sapiens	O15205 (AlphaFold model)
Ubiquitin-like modifier-activating enzyme 6	A	protein	1054	Homo sapiens	A0AVT1 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>28MJ_1 Ubiquitin D (chains B)
GPMAPNASTLTVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILK
PRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAM
IETKTGIIPETQIVTLNGKRLEDGKMMADYGIRKGNLLFLASYSIGG

Sequence of entity 2 (A), FASTA

>28MJ_2 Ubiquitin-like modifier-activating enzyme 6 (chains A)
GPMEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQK
MAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNR
AEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQC
PPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHK
LETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVF
FESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLA
TSISETLEEKPDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLY
LEAADIVESLGKPECEEFLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKN
FALLGVGTSKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKI
DAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKG
HTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNK
FWQTYSSAEEVLQKIQSGHSLEGCFQVIKLLSRRPRNWSQCVELARLKFEKYFNHKALQL
LHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPFAEEDL
SADALLNILSEVKIQEFKPSNKVVQTDETARKPDHVPISSEDERNAIFQLEKAILSNEAT
KSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTT
ATVSGLVALEMIKVTGGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRW
TVHGKEDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPGHAKRLKLTMHKLVKPTTE
KKYVDLTVSFAPDIDGDEDLPGPPVRYYFSHDTD

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
IHP	Inositol hexakisphosphate	C6 H18 O24 P6	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 O15205 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6GF1 1.93 Å, The structure of the ubiquitin-like modifier FAT10 reveals a novel targeting mechanism…
28MQ 3.04 Å, Cryo-EM structure of UBA6-FAT10Dha-UBE2Z trapped ternary complex
9E8O 3.1 Å, Nub1/Fat10-processing human 26S proteasome bound to Txnl1 with Rpt2 at top of spiral…
7PYV 3.27 Å, Crystal structure of human UBA6 in complex with the ubiquitin-like modifier FAT10
28MK 3.53 Å, Cryo-EM structure of UBA6 in complex with FAT10 in the post-thiolation state.
2MBE Backbone 1H and 15N Chemical Shift Assignments for the first domain of FAT10
6GF2 The structure of the ubiquitin-like modifier FAT10 reveals a novel targeting mechanism…

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