4ZFO: PDB entry 4ZFO

J22.9-xi: chimeric mouse/human antibody against human BCMA (CD269). Determined by X-ray diffraction at 1.9 Å resolution. Released 20 May 2015.

Method: X-ray diffraction
Resolution: 1.9 Å
Organisms: Homo sapiens, Mus musculus
Chains: 6
Atoms: 7,946
Mol. weight: 106.71 kDa
Ligands: CU, BTB
Released: 20 May 2015

Explore 4ZFO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZFO contains 41 α-helices and 90 β-strands across 6 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: 10 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	17
β-strand	10-12	3	18
β-strand	18-25	8	17
α-helix	29-31	3
β-strand	34-39	6	18
β-strand	45-51	7	18
β-strand	58-60	3	18
α-helix	62-64	3
β-strand	68-73	6	17
α-helix	74-76	3
β-strand	78-83	6	17
α-helix	88-90	3
β-strand	92-102	11	18
β-strand	105-110	6	18
β-strand	114-118	5	18
α-helix	121-123	3
β-strand	124	1	19
α-helix	125-126	2
β-strand	127-131	5	20
β-strand	142-152	11	20
β-strand	153	1	19
β-strand	158-161	4	21
α-helix	162-164	3
β-strand	170-172	3	20
α-helix	173-175	3
β-strand	176-177	2	20
β-strand	183-192	10	20
α-helix	193-195	3
β-strand	202-207	6	21
α-helix	208-210	3
β-strand	212-217	6	21

Chain B: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	12
β-strand	10-13	4	13
β-strand	19-25	7	12
β-strand	33-38	6	13
β-strand	45-49	5	13
β-strand	53-54	2	13
α-helix	55	1
β-strand	62-66	5	12
β-strand	70-75	6	12
α-helix	80-82	3
β-strand	85-90	6	13
α-helix	96	1
β-strand	97-98	2	13
β-strand	102-106	5	13
β-strand	111	1	14
α-helix	112-113	2
β-strand	114-118	5	15
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	15
β-strand	140	1	14
β-strand	145-150	6	16
β-strand	153-154	2	16
α-helix	155	1
β-strand	159-163	5	15
α-helix	164-167	4
β-strand	173-182	10	15
α-helix	183-186	4
β-strand	191-197	7	16
β-strand	205-210	6	16

Chains F and K: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	1
β-strand	20-23	4	1
α-helix	24-27	4
α-helix	35-37	3

Chain H: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	10-12	3	8
β-strand	18-25	8	7
β-strand	34-39	6	8
β-strand	45-51	7	8
β-strand	58-60	3	8
β-strand	68-73	6	7
α-helix	74-76	3
β-strand	78-83	6	7
α-helix	88-90	3
β-strand	92-102	11	8
β-strand	105-110	6	8
β-strand	111	1	7
β-strand	114-118	5	8
α-helix	121-123	3
β-strand	124	1	9
α-helix	125-126	2
β-strand	127-131	5	10
α-helix	132-134	3
β-strand	142-152	11	10
β-strand	153	1	9
β-strand	158-161	4	11
α-helix	162-164	3
β-strand	166	1	11
β-strand	170-172	3	10
α-helix	173-175	3
β-strand	176-177	2	10
β-strand	183-192	10	10
α-helix	193-195	3
β-strand	202-207	6	11
α-helix	208-210	3
β-strand	212-217	6	11

Chain L: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	2
β-strand	10-13	4	3
β-strand	19-25	7	2
β-strand	33-38	6	3
β-strand	45-49	5	3
β-strand	53-54	2	3
α-helix	55	1
β-strand	62-65	4	2
β-strand	70-75	6	2
α-helix	80-82	3
β-strand	85-90	6	3
α-helix	96	1
β-strand	97-98	2	3
β-strand	102-106	5	3
β-strand	111	1	4
α-helix	112-113	2
β-strand	114-118	5	5
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	5
β-strand	140	1	4
β-strand	145-150	6	6
β-strand	153-154	2	6
α-helix	155	1
β-strand	159-163	5	5
α-helix	164-167	4
β-strand	173-182	10	5
α-helix	183-186	4
β-strand	191-197	7	6
β-strand	205-210	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor necrosis factor receptor superfamily member 17	F, K	protein	54	Homo sapiens	Q02223 (AlphaFold model)
J22.9-xi Fab, Light Chain	L	protein	214	Mus musculus
J22.9-xi Fab, Heavy Chain	A, H	protein	221	Mus musculus
J22.9-xi Fab, Light Chain	B	protein	213	Mus musculus

Sequence of entity 1 (F, K), FASTA

>4ZFO_1 Tumor necrosis factor receptor superfamily member 17 (chains F, K)
MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNA

Sequence of entity 2 (L), FASTA

>4ZFO_2 J22.9-xi Fab, Light Chain (chains L)
DIVMTQSQRFMTTSVGDRVSVTCKASQSVDSNVAWYQQKPRQSPKALIFSASLRFSGVPA
RFTGSGSGTDFTLTISNLQSEDLAEYFCQQYNNYPLTFGAGTKLELKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEA

Sequence of entity 3 (A, H), FASTA

>4ZFO_3 J22.9-xi Fab, Heavy Chain (chains A, H)
QVQLQQSGGGLVQPGGSLKLSCAASGIDFSRYWMSWVRRAPGKGLEWIGEINPDSSTINY
APSLKDKFIISRDNAKNTLYLQMSKVRSEDTALYYCASLYYDYGDAMDYWGQGTSVTVSS
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPA

Sequence of entity 4 (B), FASTA

>4ZFO_4 J22.9-xi Fab, Light Chain (chains B)
DIVMTQSQRFMTTSVGDRVSVTCKASQSVDSNVAWYQQKPRQSPKALIFSASLRFSGVPA
RFTGSGSGTDFTLTISNLQSEDLAEYFCQQYNNYPLTFGAGTKLELKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE

Ligands and cofactors

ID	Name	Formula	Copies
CU	Copper (II) ion	Cu	3
BTB	2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol	C8 H19 N O5	2

Primary citation

Potent anti-tumor response by targeting B cell maturation antigen (BCMA) in a mouse model of multiple myeloma. Oden, F., Marino, S.F., Brand, J. et al. Mol Oncol (2015) 9:1348-1358. DOI 10.1016/j.molonc.2015.03.010 · PubMed

Other PDB entries of the same protein (UniProt Q02223 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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
12ES 3.43 Å, Cryo-EM structure of BCMA in complex with the BCMA-targeted Fab arm of linvoseltamab and…
2KN1 Solution NMR Structure of BCMA

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