9UXC: Transcription activator BRG1

The ADP-bound structure of BCL7B-containing ARP module of the human SWI/SNF complex. Determined by electron microscopy at 2.74 Å resolution. Released 6 May 2026.

Method: Electron microscopy
Resolution: 2.74 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,400
Mol. weight: 124.48 kDa
Ligands: ATP, ADP, MG
Released: 6 May 2026

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

Secondary structure: helices and β-sheets

9UXC contains 44 α-helices and 47 β-strands across 4 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	463-509	47

Chain B: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-10	3	1
β-strand	11-12	2	2
β-strand	16-18	3	2
β-strand	21	1	1
β-strand	22	1	3
β-strand	24	1	3
β-strand	30-32	3	2
α-helix	81-87	7
α-helix	88-92	5
β-strand	103-107	5	1
α-helix	113-124	12
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	4
β-strand	160-166	7	4
β-strand	169-170	2	4
β-strand	176-178	3	4
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-240	3	5
β-strand	248-250	3	5
α-helix	252-254	3
α-helix	256-259	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	4
α-helix	309-318	10
β-strand	329	1	4
α-helix	338-346	9
α-helix	351-354	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-372	4

Chain C: 24 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	15-19	5	6
β-strand	23-28	6	6
β-strand	29	1	7
β-strand	31	1	7
β-strand	36-39	4	6
β-strand	42	1	8
β-strand	43-45	3	9
β-strand	68-70	3	9
β-strand	83	1	9
β-strand	86	1	8
β-strand	89-90	2	10
β-strand	93-94	2	10
α-helix	97-106	10
α-helix	107-111	5
α-helix	116-118	3
β-strand	121-125	5	6
α-helix	131-143	13
β-strand	149-154	6	6
α-helix	155-162	8
β-strand	167-172	6	11
β-strand	178-184	7	11
β-strand	187-188	2	11
α-helix	190-192	3
β-strand	194-196	3	11
α-helix	200-213	14
α-helix	221-223	3
β-strand	224-227	4	12
α-helix	235-236	2
β-strand	238-240	3	12
α-helix	245-246	2
α-helix	249-267	19
β-strand	269	1	13
α-helix	277-280	4
α-helix	284-285	2
β-strand	286-290	5	14
β-strand	293-298	6	14
α-helix	300-303	4
α-helix	307-310	4
α-helix	312-314	3
α-helix	323-325	3
α-helix	326-335	10
α-helix	342-347	6
β-strand	349-352	4	11
β-strand	359	1	13
α-helix	361-371	11
β-strand	381-382	2	11
α-helix	387-391	5
α-helix	393-402	10
β-strand	412-413	2	6
α-helix	414-418	5
α-helix	424-428	5

Chain D: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	32-38	7	15
β-strand	45-51	7	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription activator BRG1	A	protein	101	Homo sapiens	P51532 (AlphaFold model)
Actin, cytoplasmic 1, N-terminally processed	B	protein	376	Homo sapiens	P60709 (AlphaFold model)
Actin-like protein 6A	C	protein	430	Homo sapiens	O96019 (AlphaFold model)
B-cell CLL/lymphoma 7 protein family member B	D	protein	203	Homo sapiens	Q9BQE9 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9UXC_1 Transcription activator BRG1 (chains A)
MSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAV
ATYHANTEREQKKWSHPQFEKGGGSGGGSGGGSWSHPQFEK

Sequence of entity 2 (B), FASTA

>9UXC_2 Actin, cytoplasmic 1, N-terminally processed (chains B)
MADDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKM
TQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLD
LAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS
YELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVL
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK
QEYDESGPSIVHRKCF

Sequence of entity 3 (C), FASTA

>9UXC_3 Actin-like protein 6A (chains C)
MASGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGD
KGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHP
VLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTA
IPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKR
KEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGA
ERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQS
FTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEG
GKQCVERKCP

Sequence of entity 4 (D), FASTA

>9UXC_4 B-cell CLL/lymphoma 7 protein family member B (chains D)
MASGRSVRAETRSRAKDDIKKVMAAIEKVRKWEKKWVTVGDTSLRIFKWVPVTDSKEKEK
SKSNSSAAREPNGFPSDASANSSLLLEFQDENSNQSSVSDVYQLKVDSSTNSSPSPQQSE
SLSPAHTSDFRTDDSQPPTLGQEILEEPSLPSSEVADEPPTLTKEEPVPLETQVVEEEED
SGAPPLKRFCVDQPTVPQTASES

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
MG	Magnesium ion	Mg	2

Primary citation

Structural basis for BCL7B-mediated ncBAF-nucleosome engagement. Sun, F., Zou, B., Li, H. et al. Nucleic Acids Res (2026) 54. DOI 10.1093/nar/gkag092 · PubMed

Other PDB entries of the same protein (UniProt P51532 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7TAB 1.16 Å, G-925 bound to the SMARCA4 (BRG1) Bromodomain
2GRC 1.5 Å, 1.5 A structure of bromodomain from human BRG1 protein, a central ATPase of SWI/SNF…
6ZS2 1.57 Å, Crystal Structure of the bromodomain of human transcription activator BRG1 (SMARCA4) in…
7TD9 1.61 Å, G-059 bound to the SMARCA4 (BRG1) Bromodomain
6HR2 1.76 Å, Crystal structure of PROTAC 2 in complex with the bromodomain of human SMARCA4 and…
3UVD 1.85 Å, Crystal Structure of the bromodomain of human Transcription activator BRG1 (SMARCA4) in…
5DKD 2.0 Å, Crystal structure of the bromodomain of human BRG1 (SMARCA4) in complex with PFI-3…
5EA1 2.0 Å, Crystal Structure of SMARCA4 bromodomain in complex with MPD
9DTX 2.11 Å, Crystal structure of PRT3789 in complex with the bromodomain of human BRG1 (SMARCA4) and…
7VRB 2.39 Å, Structure of the Human BRG1/SS18 complex
7VDT 2.8 Å, The motor-nucleosome module of human chromatin remodeling PBAF-nucleosome complex
9WBZ 2.9 Å, The structure of NCP-motor-ARP module of ncBAF-nucleosome complex

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