12ES: BCMA

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.

Method: Electron microscopy
Resolution: 3.43 Å
Organisms: Mus musculus, Homo sapiens
Chains: 5
Atoms: 7,049
Mol. weight: 104.76 kDa
Released: 12 Aug 2026

Explore 12ES in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 7 helices, 24 β-strands

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

Chain B: 7 helices, 21 β-strands

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

Chain C: 2 helices, 3 β-strands

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

Chain D: 4 helices, 22 β-strands

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

Chain E: 7 helices, 21 β-strands

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

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>12ES_1 Heavy chain of the Fab fragment of an anti-kappa light chain antibody REGN654 (chains A)
QVQLQQWGAGLLKPSETLSLTCAVYGGSLSDYYWTWIRQPPEKGLEWIGEINHSGSTNYA
PSLKSRVTISVDTSKNQFSLKLTSVTAADTAVYYCARTTYGYDYYFDMDVWGQGTTVTVS
SAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQS
DLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGP

Sequence of entity 2 (B), FASTA

>12ES_2 Light chain of the Fab fragment of an anti-kappa light chain antibody REGN654 (chains B)
DIQMTQSPSSLSASVGDRVTITCRASQVITNFLAWYQQTPGKVPKLLIYAASTLQSGVPS
RFSGSGSGTDFTLTISSLQPEDVATYYCQKYNYTPLTFGGGTKVEIKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRGEC

Sequence of entity 3 (C), FASTA

>12ES_3 Tumor necrosis factor receptor superfamily member 17 (chains C)
MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNAEQKLIS
EEDLGGEQKLISEEDLHHHHHH

Sequence of entity 4 (D), FASTA

>12ES_4 Heavy chain of the BCMA-targeted Fab arm of linvoseltamab (chains D)
EVQLVESGGGLVQPGGSLRLSCAASGFTFSNFWMTWVRQAPGKGLEWVANMNQDGSEKYY
VDSVKGRFTISRDNAKSSLYLQMNSLRAEDTAVYYCARDREYCISTSCYDDFDYWGQGTL
VTVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA
VLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKY

Sequence of entity 5 (E), FASTA

>12ES_5 Light chain of the BCMA-targeted Fab arm of linvoseltamab (chains E)
DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLHSGVPS
RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPPITFGQGTRLEIKRTVAAPSVFIFP
PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Primary citation

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:

4ZFO 1.9 Å, J22.9-xi: chimeric mouse/human antibody against human BCMA (CD269)
1XU2 2.35 Å, The crystal structure of APRIL bound to BCMA
8HXQ 2.4 Å, Nanobody1 in complex with human BCMA ECD
1OQD 2.6 Å, Crystal structure of sTALL-1 and BCMA
6J7W 2.6 Å, Crystal Structure of Human BCMA in complex with UniAb(TM) VH
8HXR 2.7 Å, Nanobody2 in complex with human BCMA ECD
8QYA 2.72 Å, J22.9-FNY, fully humanized, CDR optimized Fab Fragment based on chimeric J22.9-xi IgG…
12ER 2.99 Å, Cryo-EM structure of BCMA in complex with the BCMA-targeted Fab arm of teclistamab and…
8QYB 3.09 Å, J22.9-ISY, fully humanized and CDR optimized Fab Fragment based on chimeric J22.9-xi IgG…
8QY9 3.1 Å, J22.9-H, fully humanized Fab Fragment based on chimeric J22.9-xi IgG against BCMA
9MQO 3.18 Å, Crystal structure of BCMA in complex with CA10v2 Fab
2KN1 Solution NMR Structure of BCMA

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