9QII: UBA6

Structure of UBA6 (cluster 3). Determined by electron microscopy at 3.99 Å resolution. Released 29 Oct 2025.

Method: Electron microscopy
Resolution: 3.99 Å
Organism: Homo sapiens
Chains: 1
Atoms: 8,077
Mol. weight: 119.42 kDa
Ligands: IHP, ATP
Released: 29 Oct 2025

Explore 9QII in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9QII contains 57 α-helices and 52 β-strands across 1 chain. 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 B: 57 helices, 52 β-strands

Element	Residues	Length	Sheet
α-helix	41-44	4
α-helix	46-51	6
α-helix	53-59	7
β-strand	63-67	5	1
α-helix	71-83	13
β-strand	87-91	5	1
β-strand	95	1	2
α-helix	99-102	4
α-helix	109-113	5
β-strand	117	1	2
α-helix	118-129	12
β-strand	134-136	3	1
α-helix	149-153	5
β-strand	156-159	4	1
α-helix	164-176	13
α-helix	180-181	2
β-strand	182-189	8	1
β-strand	190	1	3
β-strand	192-198	7	1
β-strand	203-205	3	4
β-strand	215-217	3	5
β-strand	218-221	4	6
α-helix	227	1
β-strand	228-231	4	6
β-strand	244-251	8	5
β-strand	257	1	5
β-strand	260-262	3	5
β-strand	264-267	4	6
β-strand	270-272	3	6
α-helix	280-282	3
β-strand	284-291	8	5
β-strand	295-297	3	4
α-helix	299-301	3
α-helix	302-307	6
β-strand	311	1	1
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	3
α-helix	388-407	20
β-strand	416-420	5	1
α-helix	422-426	5
α-helix	433-436	4
α-helix	444-450	7
α-helix	452-459	8
β-strand	462-466	5	7
α-helix	470-482	13
β-strand	492-496	5	7
β-strand	500	1	8
α-helix	504-507	4
α-helix	514-516	3
β-strand	520	1	8
α-helix	521-532	12
β-strand	538-541	4	7
α-helix	547-551	5
α-helix	555-560	6
β-strand	563-566	4	7
α-helix	571-584	14
β-strand	588-594	7	7
β-strand	597-603	7	7
β-strand	608	1	9
α-helix	621-623	3
α-helix	624-629	6
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	10
β-strand	733	1	10
α-helix	752-768	17
α-helix	780-788	9
α-helix	790-795	6
α-helix	814-817	4
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	895-913	19
β-strand	922-927	6	7
β-strand	932-937	6	7
α-helix	938-939	2
β-strand	940	1	9
α-helix	941	1
β-strand	944-947	4	11
β-strand	950-952	3	11
β-strand	958-961	4	12
β-strand	967	1	13
α-helix	968-979	12
β-strand	983	1	14
β-strand	986-988	3	15
β-strand	991-994	4	15
α-helix	1002-1006	5
β-strand	1008	1	13
α-helix	1009-1012	4
β-strand	1021-1024	4	12
β-strand	1025	1	15
β-strand	1027-1028	2	14
β-strand	1033	1	16
β-strand	1035	1	16
α-helix	1037	1
β-strand	1038-1039	2	14
β-strand	1043-1046	4	12

Molecules and chains

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

Sequence of entity 1 (B), FASTA

>9QII_1 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

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

UBA6 specificity for ubiquitin E2 conjugating enzymes reveals a priority mechanism of BIRC6. Riechmann, C., Ellison, C.J., Anderson, J.W. et al. Nat Struct Mol Biol (2026) 33:464-478. DOI 10.1038/s41594-025-01717-z · PubMed

Other PDB entries of the same protein (UniProt A0AVT1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7SOL 2.25 Å, Crystal Structures of the bispecific ubiquitin/FAT10 activating enzyme, Uba6
7PVN 2.71 Å, Crystal Structure of Human UBA6 in Complex with ATP
9YKV 2.73 Å, Cryo-EM structure of double-loaded human UBA6-UBE2Z-FAT10(t)/FAT10(a) thioester mimetic…
28MJ 2.77 Å, Cryo-EM structure of UBA6 in complex with FAT10 in the pre-adenylation state.
28MO 3.01 Å, Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (singly loaded)
28MQ 3.04 Å, Cryo-EM structure of UBA6-FAT10Dha-UBE2Z trapped ternary complex
9QH5 3.09 Å, Consensus structure of UBA6-UbDha-BIRC6 trapped ternary complex (doubly loaded)
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.
7PYV 3.27 Å, Crystal structure of human UBA6 in complex with the ubiquitin-like modifier FAT10
9QIC 3.29 Å, Consensus structure of UBA6

Browse structure collections

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