The apo structure of BCL7B-containing ARP module of the human SWI/SNF complex. Determined by electron microscopy at 2.92 Å resolution. Released 6 May 2026.
Explore 9UXB in 3D Show helices and sheets RCSB PDB PDBe
9UXB contains 46 α-helices and 45 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 465-513 | 49 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35 | 1 | 2 |
| β-strand | 54 | 1 | 2 |
| α-helix | 56-60 | 5 | |
| β-strand | 68 | 1 | 2 |
| β-strand | 71-72 | 2 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 82-87 | 6 | |
| α-helix | 88-93 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-145 | 9 | |
| 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 | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-226 | 4 | |
| β-strand | 238-242 | 5 | 5 |
| β-strand | 246-250 | 5 | 5 |
| α-helix | 252-255 | 4 | |
| α-helix | 258-261 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-295 | 9 | |
| β-strand | 297-300 | 4 | 4 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 4 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-346 | 9 | |
| α-helix | 352-354 | 3 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-373 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-17 | 4 | 6 |
| β-strand | 22-27 | 6 | 6 |
| β-strand | 35-38 | 4 | 6 |
| β-strand | 41 | 1 | 7 |
| β-strand | 42-44 | 3 | 8 |
| β-strand | 67-69 | 3 | 8 |
| α-helix | 71-75 | 5 | |
| β-strand | 85 | 1 | 7 |
| β-strand | 88-89 | 2 | 9 |
| β-strand | 92-93 | 2 | 9 |
| α-helix | 96-105 | 10 | |
| α-helix | 106-111 | 6 | |
| β-strand | 120-124 | 5 | 6 |
| α-helix | 130-139 | 10 | |
| α-helix | 140-144 | 5 | |
| β-strand | 148-153 | 6 | 6 |
| α-helix | 154-161 | 8 | |
| β-strand | 167-171 | 5 | 10 |
| β-strand | 177-183 | 7 | 10 |
| β-strand | 186-187 | 2 | 10 |
| β-strand | 193-195 | 3 | 10 |
| α-helix | 199-212 | 14 | |
| α-helix | 220-222 | 3 | |
| β-strand | 223-226 | 4 | 11 |
| β-strand | 237-239 | 3 | 11 |
| α-helix | 240 | 1 | |
| α-helix | 244-247 | 4 | |
| α-helix | 248-265 | 18 | |
| β-strand | 268 | 1 | 12 |
| α-helix | 276-280 | 5 | |
| α-helix | 283-284 | 2 | |
| β-strand | 285-288 | 4 | 13 |
| β-strand | 294-297 | 4 | 13 |
| α-helix | 306-309 | 4 | |
| α-helix | 325-334 | 10 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-345 | 5 | |
| β-strand | 348-351 | 4 | 10 |
| α-helix | 353-356 | 4 | |
| β-strand | 358 | 1 | 12 |
| α-helix | 360-371 | 12 | |
| β-strand | 380 | 1 | 10 |
| α-helix | 386-390 | 5 | |
| α-helix | 392-401 | 10 | |
| β-strand | 411-412 | 2 | 6 |
| α-helix | 413-417 | 5 | |
| α-helix | 423-427 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31-37 | 7 | 14 |
| β-strand | 44-50 | 7 | 14 |
| 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) |
>9UXB_1 Transcription activator BRG1 (chains A) MSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAV ATYHANTEREQKKWSHPQFEKGGGSGGGSGGGSWSHPQFEK
>9UXB_2 Actin, cytoplasmic 1, N-terminally processed (chains B) MADDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ SKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKM TQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLD LAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKS YELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVL SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK QEYDESGPSIVHRKCF
>9UXB_3 Actin-like protein 6A (chains C) MASGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGD KGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHP VLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTA IPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKR KEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGA ERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQS FTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEG GKQCVERKCP
>9UXB_4 B-cell CLL/lymphoma 7 protein family member B (chains D) MASGRSVRAETRSRAKDDIKKVMAAIEKVRKWEKKWVTVGDTSLRIFKWVPVTDSKEKEK SKSNSSAAREPNGFPSDASANSSLLLEFQDENSNQSSVSDVYQLKVDSSTNSSPSPQQSE SLSPAHTSDFRTDDSQPPTLGQEILEEPSLPSSEVADEPPTLTKEEPVPLETQVVEEEED SGAPPLKRFCVDQPTVPQTASES
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:
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