9SQV: ARISCdC(E33A):K63-Ub4 complex

Cryo-EM structure of the ARISCdC(E33A):K63-Ub4 complex (Composite map). Determined by electron microscopy at 3.21 Å resolution. Released 5 Aug 2026.

Method: Electron microscopy
Resolution: 3.21 Å
Organism: Homo sapiens
Chains: 8
Atoms: 12,545
Mol. weight: 244.88 kDa
Ligands: ZN
Released: 5 Aug 2026

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

Secondary structure: helices and β-sheets

9SQV contains 55 α-helices and 87 β-strands across 8 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: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	9
α-helix	16-26	11
β-strand	35-42	8	9
β-strand	72-79	8	9
β-strand	84-85	2	5
β-strand	90-92	3	5
α-helix	94-111	18
β-strand	116-125	10	9
α-helix	135-141	7
α-helix	142-144	3
β-strand	150-156	7	9
β-strand	166	1	9
β-strand	169-172	4	9
β-strand	173-174	2	11
β-strand	212-213	2	11
β-strand	216-219	4	9
α-helix	226-232	7
α-helix	235-252	18
α-helix	258-276	19
α-helix	280-307	28

Chain B: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	6
α-helix	16-26	11
β-strand	35-41	7	6
β-strand	72-80	9	6
α-helix	94-111	18
β-strand	116-122	7	6
α-helix	133-143	11
β-strand	151-155	5	6
β-strand	166-173	8	6
β-strand	216-219	4	6
α-helix	226-232	7
α-helix	234-252	19
α-helix	258-275	18
α-helix	276-280	5
α-helix	281-307	27

Chain C: 8 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	6
α-helix	12-24	13
β-strand	29-39	11	6
β-strand	57-67	11	6
β-strand	74	1	7
β-strand	80	1	7
α-helix	82-88	7
β-strand	95-102	8	6
α-helix	112-123	12
β-strand	131-139	9	6
β-strand	147-154	8	6
α-helix	156-158	3
β-strand	166-169	4	6
α-helix	171-173	3
α-helix	189-197	9
α-helix	199-202	4
β-strand	203	1	8
β-strand	209	1	8
α-helix	210-249	40

Chain D: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	9
α-helix	12-22	11
β-strand	30-37	8	9
β-strand	59-67	9	9
α-helix	82-88	7
β-strand	95-102	8	9
α-helix	112-125	14
β-strand	131-139	9	9
β-strand	147-154	8	9
β-strand	166-169	4	9
α-helix	183-184	2
α-helix	189-197	9
α-helix	199-202	4
β-strand	203	1	10
β-strand	209	1	10
α-helix	210-250	41

Chain E: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	10	1	20
α-helix	15-23	9
β-strand	37-41	5	21
β-strand	53	1	20
β-strand	55-59	5	21
β-strand	62	1	22
β-strand	65	1	22
β-strand	68-72	5	21
β-strand	83-85	3	21
α-helix	96-98	3
α-helix	100-103	4
α-helix	112-131	20
α-helix	139-144	6
α-helix	149-152	4
β-strand	156-158	3	23
α-helix	161-163	3
β-strand	172-174	3	23
β-strand	175	1	24
β-strand	203	1	24
β-strand	204	1	25
β-strand	206	1	23
β-strand	218	1	25
α-helix	223-228	6
α-helix	236-241	6
α-helix	249-265	17

Chain F: 11 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	7-9	3
β-strand	10	1	12
α-helix	12-14	3
α-helix	15-23	9
β-strand	36-41	6	13
β-strand	53	1	12
β-strand	55-59	5	13
β-strand	62	1	14
β-strand	65	1	14
β-strand	68-72	5	13
α-helix	81-82	2
β-strand	83-85	3	13
α-helix	100-103	4
α-helix	112-128	17
α-helix	129-132	4
α-helix	138-140	3
α-helix	141-147	7
β-strand	157	1	15
β-strand	161-162	2	16
β-strand	167-168	2	16
β-strand	171-172	2	17
β-strand	173	1	15
β-strand	175-176	2	18
β-strand	202-203	2	18
β-strand	204	1	19
β-strand	206-207	2	17
β-strand	218	1	19
α-helix	223-229	7
α-helix	246-260	15

Chain G: 1 helix, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	1
β-strand	12-16	5	1
β-strand	22	1	2
α-helix	23-33	11
β-strand	41-45	5	1
β-strand	48-49	2	1
β-strand	55	1	2
β-strand	66-71	6	1

Chain H: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	3
β-strand	12-16	5	3
β-strand	22	1	4
α-helix	23-31	9
β-strand	42-45	4	3
β-strand	48-49	2	3
β-strand	55	1	4
α-helix	57-59	3
β-strand	66-70	5	3
β-strand	73-75	3	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin	G, H	protein	76	Homo sapiens	P0CG48 (AlphaFold model)
BRCA1-A complex subunit Abraxas 1	C, D	protein	302	Homo sapiens	Q6UWZ7 (AlphaFold model)
Lys-63-specific deubiquitinase BRCC36	A, B	protein	316	Homo sapiens	P46736 (AlphaFold model)
BRISC and BRCA1-A complex member 2	E, F	protein	385	Homo sapiens	Q9NXR7 (AlphaFold model)

Sequence of entity 1 (G, H), FASTA

>9SQV_1 Ubiquitin (chains G, H)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Sequence of entity 2 (C, D), FASTA

>9SQV_2 BRCA1-A complex subunit Abraxas 1 (chains C, D)
MWSHPQFEKGGGSGGGSGGSAWSHPQFEKLEVLFQGTMEGESTSAVLSGFVLGALAFQHL
NTDSDTEGFLLGEVKGEAKNSITDSQMDDVEVVYTIDIQKYIPCYQLFSFYNSSGEVNEQ
ALKKILSNVKKNVVGWYKFRRHSDQIMTFRERLLHKNLQEHFSNQDLVFLLLTPSIITES
CSTHRLEHSLYKPQKGLFHRVPLVVANLGMSEQLGYKTVSGSCMSTGFSRAVQTHSSKFF
EEDGSLKEVHKINEMYASLQEELKSICKKVEDSEQAVDKLVKDVNRLKREIEKRRGAQIQ
AA

Sequence of entity 3 (A, B), FASTA

>9SQV_3 Lys-63-specific deubiquitinase BRCC36 (chains A, B)
MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEAVMGLCIGELNDDTRSDSKFAYTGTEMR
TVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGW
YHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQK
SSESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILC
QEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQE
LQQEKEELMQELSSLE

Sequence of entity 4 (E, F), FASTA

>9SQV_4 BRISC and BRCA1-A complex member 2 (chains E, F)
GAMSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKL
HIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVK
ELVQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLP
VDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIP
AFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGTGVVEYDAEGFTKLT
LLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEM
AKRAKAYFKTFVPQFQEAAFANGKL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Mechanism of K63-linked polyubiquitin recognition and cleavage by the BRCA1-A complex. Foglizzo, M., Datta, A., Degtjarik, O. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-75795-y · PubMed

Other PDB entries of the same protein (UniProt P0CG48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Q00 0.85 Å, TDP2 UBA Domain Bound to Ubiquitin at 0.85 Angstroms Resolution, Crystal Form 1
1OGW 1.32 Å, Synthetic Ubiquitin with fluoro-Leu at 50 and 67
5NL4 1.32 Å, Crystal structure of Zn1.3-E16V human ubiquitin (hUb) mutant adduct, from a solution 35…
2GBJ 1.35 Å, Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.
4HK2 1.4 Å, U7Ub25.2540
9FJ3 1.4 Å, Structure of ubiquitin bound of coiled-coil UIM form 2
1XD3 1.45 Å, Crystal structure of UCHL3-UbVME complex
4IUM 1.45 Å, Equine arteritis virus papain-like protease 2 (PLP2) covalently bound to ubiquitin
7UV5 1.45 Å, The crystal structure of Papain-Like Protease of SARS CoV-2, C111S/D286N mutant, in…
5NLF 1.5 Å, Crystal structure of Zn2.7-E16V human ubiquitin (hUb) mutant adduct, from a solution 100…
9F6G 1.5 Å, Human USP30 chimera bound to Ubiquitin-PA
9OVX 1.5 Å, Crystal structure of ubiquitin K27M mutant

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