9SQW: ARISCdC(E33A):K63-Ub7 complex

Cryo-EM structure of the ARISCdC(E33A):K63-Ub7 complex (Composite map). Determined by electron microscopy at 3.2 Å resolution. Released 5 Aug 2026.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 10
Atoms: 13,761
Mol. weight: 262.03 kDa
Ligands: ZN
Released: 5 Aug 2026

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

Secondary structure: helices and β-sheets

9SQW contains 54 α-helices and 101 β-strands across 10 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: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	14
α-helix	16-26	11
β-strand	35-42	8	14
β-strand	71-79	9	14
β-strand	84-85	2	6
β-strand	90-91	2	6
α-helix	94-111	18
β-strand	116-125	10	14
α-helix	133-143	11
β-strand	150-160	11	14
β-strand	165-176	12	14
β-strand	210-213	4	14
β-strand	216-219	4	14
α-helix	226-251	26
α-helix	258-275	18
α-helix	276-280	5
α-helix	281-315	35

Chain B: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	17
α-helix	16-26	11
β-strand	35-40	6	18
β-strand	42	1	17
β-strand	72-74	3	17
β-strand	76-79	4	18
α-helix	94-111	18
β-strand	116-122	7	18
α-helix	133-143	11
β-strand	151-153	3	18
β-strand	166-169	4	1
β-strand	171-173	3	18
β-strand	213	1	18
β-strand	216-219	4	17
α-helix	226-252	27
α-helix	258-275	18
α-helix	276-280	5
α-helix	281-314	34

Chain C: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	1
α-helix	12-24	13
β-strand	30-44	15	1
β-strand	52-66	15	1
β-strand	74	1	2
α-helix	79	1
β-strand	80	1	2
α-helix	81	1
α-helix	82-88	7
β-strand	95-102	8	1
α-helix	112-122	11
β-strand	131-135	5	1
β-strand	138	1	1
β-strand	148-154	7	1
α-helix	156-158	3
β-strand	163-164	2	1
β-strand	166-169	4	1
α-helix	171-173	3
α-helix	190-197	8
β-strand	203	1	3
β-strand	209	1	3
α-helix	210-255	46

Chain D: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	14
α-helix	12-23	12
β-strand	30-39	10	14
β-strand	57-67	11	14
β-strand	74	1	15
β-strand	80	1	15
α-helix	82-88	7
β-strand	95-102	8	14
α-helix	114-125	12
β-strand	131-139	9	14
β-strand	147-154	8	14
β-strand	163	1	14
β-strand	166-169	4	14
α-helix	171-173	3
α-helix	189-197	9
α-helix	199-202	4
β-strand	203	1	16
β-strand	209	1	16
α-helix	210-256	47

Chain E: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10	1	19
α-helix	15-23	9
β-strand	36-41	6	20
β-strand	53	1	19
β-strand	55-62	8	20
β-strand	65-72	8	20
β-strand	83-85	3	20
α-helix	100-103	4
α-helix	112-132	21
α-helix	139-147	9
β-strand	157-159	3	21
β-strand	171-173	3	21
β-strand	175-176	2	22
β-strand	202-203	2	22
β-strand	204	1	23
β-strand	218	1	23
α-helix	223-228	6
α-helix	246-248	3
α-helix	249-253	5

Chain F: 6 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	6-9	4
β-strand	10	1	24
α-helix	15-24	10
β-strand	36-41	6	25
β-strand	53	1	24
β-strand	55-61	7	25
β-strand	66-72	7	25
β-strand	83-85	3	25
α-helix	96-98	3
α-helix	100-103	4
α-helix	112-133	22
α-helix	138-146	9
β-strand	156-158	3	26
β-strand	172-175	4	26
β-strand	203-206	4	26
β-strand	207	1	27
β-strand	215	1	27
β-strand	218	1	26

Chain G: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	7
β-strand	12-16	5	7
β-strand	22	1	8
α-helix	23-33	11
β-strand	43-45	3	7
β-strand	48-49	2	7
β-strand	55	1	8
α-helix	57-59	3
β-strand	66-69	4	7

Chain H: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	4
β-strand	12-16	5	4
β-strand	22	1	5
α-helix	23-33	11
β-strand	42-45	4	4
β-strand	48-49	2	4
β-strand	55	1	5
α-helix	56-59	4
β-strand	66-70	5	4
β-strand	74-75	2	6

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
BRCA1-A complex subunit Abraxas 1	C, D	protein	302	Homo sapiens	Q6UWZ7 (AlphaFold model)
Ubiquitin	G, H, I, J	protein	76	Homo sapiens	P0CG48 (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 (C, D), FASTA

>9SQW_1 BRCA1-A complex subunit Abraxas 1 (chains C, D)
MWSHPQFEKGGGSGGGSGGSAWSHPQFEKLEVLFQGTMEGESTSAVLSGFVLGALAFQHL
NTDSDTEGFLLGEVKGEAKNSITDSQMDDVEVVYTIDIQKYIPCYQLFSFYNSSGEVNEQ
ALKKILSNVKKNVVGWYKFRRHSDQIMTFRERLLHKNLQEHFSNQDLVFLLLTPSIITES
CSTHRLEHSLYKPQKGLFHRVPLVVANLGMSEQLGYKTVSGSCMSTGFSRAVQTHSSKFF
EEDGSLKEVHKINEMYASLQEELKSICKKVEDSEQAVDKLVKDVNRLKREIEKRRGAQIQ
AA

Sequence of entity 2 (G, H, I, J), FASTA

>9SQW_2 Ubiquitin (chains G, H, I, J)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Sequence of entity 3 (A, B), FASTA

>9SQW_3 Lys-63-specific deubiquitinase BRCC36 (chains A, B)
MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEAVMGLCIGELNDDTRSDSKFAYTGTEMR
TVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGW
YHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQK
SSESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILC
QEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQE
LQQEKEELMQELSSLE

Sequence of entity 4 (E, F), FASTA

>9SQW_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 Q6UWZ7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4Y2G 2.5 Å, Structure of BRCA1 BRCT domains in complex with Abraxas single phosphorylated peptide
9SQY 2.92 Å, Cryo-EM structure of the ARISC(E33A)-RAP80:K63-Ub7 complex (Composite map)
9SMP 3.0 Å, BRCA1-A complex bound to K63-polyUbATA - open form double State P
9SMN 3.2 Å, BRCA1-A complex bound to K63-polyUbATA - open form StateC StateP
9SNA 3.2 Å, BRCA1-A complex bound to K63-diUbATA - open form StateC StateP
9SQV 3.21 Å, Cryo-EM structure of the ARISCdC(E33A):K63-Ub4 complex (Composite map)
9SMR 3.25 Å, Structure of apo BRCA1-A complex in presence of K63-oligoUbATA
9SMS 3.3 Å, BRCA1-A complex: Ubiquitin bound to BRE at the wrist site (focused 3D class)
9SO9 3.4 Å, BRCA1-A complex bound to K63-oligoUbATA - closed form StateC*
4JLU 3.5 Å, Crystal structure of BRCA1 BRCT with doubly phosphorylated Abraxas
4Y18 3.5 Å, Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide
4U4A 3.51 Å, Complex Structure of BRCA1 BRCT with singly phospho Abraxas

Browse structure collections

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