9QIC: Consensus structure of UBA6

Consensus structure of UBA6. Determined by electron microscopy at 3.29 Å resolution. Released 29 Oct 2025.

Method: Electron microscopy
Resolution: 3.29 Å
Organism: Homo sapiens
Chains: 1
Atoms: 8,077
Mol. weight: 119.42 kDa
Ligands: IHP, ATP
Released: 29 Oct 2025

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

Secondary structure: helices and β-sheets

9QIC contains 65 α-helices and 48 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: 65 helices, 48 β-strands

Element	Residues	Length	Sheet
α-helix	41-51	11
α-helix	53-59	7
β-strand	63-67	5	1
α-helix	71-83	13
β-strand	87-91	5	1
α-helix	94	1
β-strand	95	1	2
α-helix	96	1
α-helix	98-102	5
α-helix	109-114	6
β-strand	117	1	2
α-helix	118-127	10
β-strand	134-138	5	1
α-helix	149-153	5
β-strand	156-159	4	1
α-helix	164-175	12
α-helix	180-181	2
β-strand	182-189	8	1
β-strand	190	1	3
β-strand	192-198	7	1
β-strand	202-205	4	4
α-helix	211-214	4
β-strand	215-217	3	5
β-strand	218-221	4	6
β-strand	227-231	5	6
α-helix	232	1
β-strand	244-248	5	5
α-helix	254-256	3
β-strand	260-262	3	5
β-strand	264-267	4	6
β-strand	270-274	5	6
α-helix	280-282	3
β-strand	287-291	5	5
β-strand	295-298	4	4
α-helix	302-305	4
β-strand	311-312	2	1
α-helix	313	1
α-helix	321-339	19
α-helix	342-344	3
α-helix	348-364	17
α-helix	369-371	3
α-helix	373-381	9
β-strand	386	1	3
α-helix	388-407	20
α-helix	411-413	3
β-strand	416-417	2	1
β-strand	420	1	1
α-helix	422-426	5
α-helix	433-436	4
α-helix	444-459	16
β-strand	462-466	5	7
α-helix	470-482	13
β-strand	492-496	5	7
β-strand	500	1	8
α-helix	503-507	5
α-helix	514-516	3
β-strand	520	1	8
α-helix	521-532	12
β-strand	538-541	4	7
α-helix	547-549	3
α-helix	555-560	6
β-strand	563-566	4	7
α-helix	572-584	13
β-strand	588-594	7	7
β-strand	597-603	7	7
β-strand	608	1	9
α-helix	616-619	4
α-helix	621-623	3
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	10
β-strand	733	1	10
α-helix	752-769	18
α-helix	775-778	4
α-helix	780-788	9
α-helix	790-795	6
α-helix	813-817	5
α-helix	818-833	16
α-helix	840-842	3
α-helix	845-847	3
α-helix	858-872	15
α-helix	875-877	3
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	7
β-strand	932-937	6	7
α-helix	938-939	2
β-strand	940	1	9
α-helix	941-943	3
β-strand	944-945	2	11
β-strand	951-952	2	11
β-strand	958-961	4	12
β-strand	967	1	13
α-helix	968-978	11
β-strand	985-988	4	14
β-strand	991-994	4	14
α-helix	1002-1006	5
β-strand	1008	1	13
α-helix	1009-1012	4
β-strand	1021-1024	4	12
β-strand	1025-1028	4	14
α-helix	1036-1037	2
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

>9QIC_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
9XGB 3.3 Å, UBA6-BIRC6 ubc-ubt

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