Cryo-EM structure of BCMA in complex with the BCMA-targeted Fab arm of linvoseltamab and the Fab fragment of an anti-kappa light chain antibody REGN654. Determined by electron microscopy at 3.43 Å resolution. Released 12 Aug 2026.
Explore 12ES in 3D Show helices and sheets RCSB PDB PDBe
12ES contains 27 α-helices and 91 β-strands across 5 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 |
|---|---|---|---|
| β-strand | 3-8 | 6 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 17-25 | 9 | 1 |
| β-strand | 33-39 | 7 | 3 |
| β-strand | 46-51 | 6 | 3 |
| β-strand | 57-59 | 3 | 3 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-98 | 8 | 3 |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 106-107 | 2 | 4 |
| β-strand | 111 | 1 | 3 |
| β-strand | 115-117 | 3 | 3 |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 122-124 | 3 | |
| β-strand | 125 | 1 | 5 |
| β-strand | 128-132 | 5 | 6 |
| α-helix | 133-135 | 3 | |
| β-strand | 143-153 | 11 | 6 |
| β-strand | 154 | 1 | 5 |
| β-strand | 159-162 | 4 | 7 |
| α-helix | 163-165 | 3 | |
| β-strand | 171-173 | 3 | 6 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 6 |
| β-strand | 182-192 | 11 | 6 |
| β-strand | 202-207 | 6 | 7 |
| β-strand | 212-217 | 6 | 7 |
| α-helix | 220-222 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 8 |
| β-strand | 10-14 | 5 | 9 |
| β-strand | 19-25 | 7 | 8 |
| β-strand | 34-38 | 5 | 9 |
| β-strand | 45-49 | 5 | 9 |
| β-strand | 53-54 | 2 | 9 |
| β-strand | 62-67 | 6 | 8 |
| β-strand | 70-75 | 6 | 8 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-89 | 5 | 9 |
| β-strand | 98 | 1 | 9 |
| β-strand | 102-107 | 6 | 9 |
| β-strand | 111 | 1 | 10 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 11 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 11 |
| β-strand | 140 | 1 | 10 |
| β-strand | 144-150 | 7 | 12 |
| β-strand | 153-154 | 2 | 12 |
| β-strand | 159-163 | 5 | 11 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 11 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-198 | 8 | 12 |
| β-strand | 201-210 | 10 | 12 |
| α-helix | 211-213 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-15 | 4 | 13 |
| β-strand | 20-23 | 4 | 13 |
| α-helix | 24-27 | 4 | |
| β-strand | 32 | 1 | 14 |
| α-helix | 35-45 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 15 |
| β-strand | 11-12 | 2 | 16 |
| β-strand | 17-25 | 9 | 15 |
| β-strand | 33-39 | 7 | 14 |
| β-strand | 45-51 | 7 | 14 |
| β-strand | 58-60 | 3 | 14 |
| β-strand | 68-73 | 6 | 15 |
| β-strand | 78-84 | 7 | 15 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-104 | 13 | 14 |
| β-strand | 107-115 | 9 | 14 |
| β-strand | 119-121 | 3 | 14 |
| β-strand | 122-123 | 2 | 16 |
| β-strand | 129 | 1 | 17 |
| β-strand | 132-136 | 5 | 18 |
| β-strand | 147-157 | 11 | 18 |
| β-strand | 158 | 1 | 17 |
| β-strand | 163-166 | 4 | 19 |
| α-helix | 167-169 | 3 | |
| β-strand | 176-177 | 2 | 18 |
| α-helix | 178-180 | 3 | |
| β-strand | 181-182 | 2 | 18 |
| β-strand | 188-197 | 10 | 18 |
| α-helix | 198-200 | 3 | |
| β-strand | 206-212 | 7 | 19 |
| β-strand | 217-223 | 7 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 20 |
| β-strand | 10-12 | 3 | 21 |
| β-strand | 19-25 | 7 | 20 |
| β-strand | 33-38 | 6 | 21 |
| β-strand | 45-49 | 5 | 21 |
| β-strand | 53-54 | 2 | 21 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 20 |
| β-strand | 70-75 | 6 | 20 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 21 |
| β-strand | 99 | 1 | 21 |
| β-strand | 103-106 | 4 | 21 |
| β-strand | 112 | 1 | 22 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 23 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-127 | 5 | |
| β-strand | 130-140 | 11 | 23 |
| β-strand | 141 | 1 | 22 |
| β-strand | 146-151 | 6 | 24 |
| β-strand | 155 | 1 | 24 |
| β-strand | 160-164 | 5 | 23 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 23 |
| α-helix | 184-187 | 4 | |
| β-strand | 192-198 | 7 | 24 |
| β-strand | 206-211 | 6 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heavy chain of the Fab fragment of an anti-kappa light chain antibody REGN654 | A | protein | 223 | Mus musculus | |
| Light chain of the Fab fragment of an anti-kappa light chain antibody REGN654 | B | protein | 214 | Mus musculus | |
| Tumor necrosis factor receptor superfamily member 17 | C | protein | 82 | Homo sapiens | Q02223 (AlphaFold model) |
| Heavy chain of the BCMA-targeted Fab arm of linvoseltamab | D | protein | 227 | Homo sapiens | |
| Light chain of the BCMA-targeted Fab arm of linvoseltamab | E | protein | 215 | Homo sapiens |
>12ES_1 Heavy chain of the Fab fragment of an anti-kappa light chain antibody REGN654 (chains A) QVQLQQWGAGLLKPSETLSLTCAVYGGSLSDYYWTWIRQPPEKGLEWIGEINHSGSTNYA PSLKSRVTISVDTSKNQFSLKLTSVTAADTAVYYCARTTYGYDYYFDMDVWGQGTTVTVS SAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQS DLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGP
>12ES_2 Light chain of the Fab fragment of an anti-kappa light chain antibody REGN654 (chains B) DIQMTQSPSSLSASVGDRVTITCRASQVITNFLAWYQQTPGKVPKLLIYAASTLQSGVPS RFSGSGSGTDFTLTISSLQPEDVATYYCQKYNYTPLTFGGGTKVEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRGEC
>12ES_3 Tumor necrosis factor receptor superfamily member 17 (chains C) MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNAEQKLIS EEDLGGEQKLISEEDLHHHHHH
>12ES_4 Heavy chain of the BCMA-targeted Fab arm of linvoseltamab (chains D) EVQLVESGGGLVQPGGSLRLSCAASGFTFSNFWMTWVRQAPGKGLEWVANMNQDGSEKYY VDSVKGRFTISRDNAKSSLYLQMNSLRAEDTAVYYCARDREYCISTSCYDDFDYWGQGTL VTVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKY
>12ES_5 Light chain of the BCMA-targeted Fab arm of linvoseltamab (chains E) DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLHSGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPPITFGQGTRLEIKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
DISTINCT EPITOPE ENGAGEMENT CONFERS DIFFERENTIAL ACTIVITY OF LINVOSELTAMAB VERSUS TECLISTAMAB ACROSS BCMA MUTATIONS. Zhou, Y., Sineshchekova, O., Lee, K. et al. Blood Adv (2026). DOI 10.1182/bloodadvances.2026020381 · PubMed
Other PDB entries of the same protein (UniProt Q02223 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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