30AF: Complex between IgE-Fc and anti-IgE Fab aeFab98

Complex between IgE-Fc and anti-IgE Fab aeFab98. Determined by X-ray diffraction at 2.4 Å resolution. Released 2 Sept 2026.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Homo sapiens, Oryctolagus cuniculus
Chains: 4
Atoms: 8,321
Mol. weight: 121.4 kDa
Released: 2 Sept 2026

Explore 30AF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

30AF contains 44 α-helices and 98 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: 17 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	230-232	3
β-strand	233-239	7	1
α-helix	240-241	2
α-helix	246-248	3
β-strand	250-259	11	1
β-strand	265-270	6	8
β-strand	273-274	2	8
α-helix	277-279	3
β-strand	280-287	8	1
β-strand	290-300	11	1
α-helix	301-304	4
β-strand	310-316	7	8
β-strand	319-325	7	8
α-helix	327-330	4
β-strand	337-340	4	9
α-helix	345	1
α-helix	346-350	5
β-strand	355-363	9	9
β-strand	371-376	6	10
α-helix	384-385	2
β-strand	386-391	6	9
β-strand	397-404	8	9
α-helix	407-411	5
β-strand	416-421	6	10
β-strand	429-433	5	10
α-helix	435-437	3
β-strand	441	1	11
α-helix	442-443	2
β-strand	444-449	6	12
α-helix	450-452	3
β-strand	453	1	13
β-strand	456	1	13
β-strand	459-469	11	12
β-strand	470	1	11
β-strand	475-480	6	14
β-strand	483-484	2	14
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	12
α-helix	493-495	3
β-strand	496-497	2	12
β-strand	503-512	10	12
α-helix	513-518	6
β-strand	522-527	6	14
β-strand	536-541	6	14

Chain B: 14 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	231-232	2
β-strand	233-239	7	1
α-helix	240-241	2
β-strand	250-257	9	1
β-strand	264-270	7	2
β-strand	273-274	2	2
β-strand	281-284	4	1
β-strand	292-300	9	1
α-helix	301-304	4
β-strand	310-316	7	2
β-strand	319-325	7	2
α-helix	328-331	4
β-strand	336-340	5	3
α-helix	341-344	4
α-helix	345	1
α-helix	346-351	6
β-strand	355-362	8	3
β-strand	371-376	6	4
β-strand	386-391	6	3
β-strand	397-404	8	3
α-helix	407-411	5
β-strand	416-421	6	4
β-strand	429-433	5	4
β-strand	441	1	5
α-helix	442-443	2
β-strand	444-449	6	6
α-helix	450-453	4
β-strand	459-469	11	6
β-strand	470	1	5
β-strand	475-480	6	7
β-strand	483-484	2	7
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	6
α-helix	493-495	3
β-strand	496-497	2	6
β-strand	503-512	10	6
α-helix	513-518	6
β-strand	522-527	6	7
β-strand	536-541	6	7

Chain H: 6 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	15
β-strand	11-12	2	16
β-strand	18-25	8	15
β-strand	34-40	7	17
β-strand	46-53	8	17
β-strand	59-61	3	17
β-strand	69-73	5	15
β-strand	78-83	6	15
α-helix	88-90	3
β-strand	92-99	8	17
β-strand	108-111	4	17
β-strand	115-117	3	17
β-strand	118-119	2	16
α-helix	122-124	3
β-strand	125	1	18
α-helix	126-127	2
β-strand	128-132	5	19
β-strand	143-153	11	19
β-strand	154	1	18
β-strand	159-162	4	20
α-helix	163-165	3
β-strand	167	1	20
β-strand	171-173	3	19
α-helix	174-176	3
β-strand	177-178	2	19
β-strand	184-193	10	19
β-strand	200-205	6	20
α-helix	206-208	3
β-strand	210-215	6	20

Chain L: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	21
β-strand	10-14	5	22
β-strand	19-25	7	21
β-strand	33-38	6	22
β-strand	45-49	5	22
β-strand	53-54	2	22
α-helix	55	1
β-strand	62-67	6	21
β-strand	70-75	6	21
α-helix	80-82	3
β-strand	84-90	7	22
β-strand	101	1	22
β-strand	105-110	6	22
β-strand	114	1	23
α-helix	115-116	2
β-strand	117-121	5	24
α-helix	122-124	3
α-helix	128-130	3
β-strand	132-142	11	24
β-strand	143	1	23
β-strand	147-152	6	25
β-strand	155-156	2	25
β-strand	161-165	5	24
α-helix	166-169	4
β-strand	175-184	10	24
α-helix	185-189	5
β-strand	193-200	8	25
β-strand	203-210	8	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform 1 of Immunoglobulin heavy constant epsilon	A, B	protein	327	Homo sapiens	P01854 (AlphaFold model)
aeFab98 heavy chain	H	protein	216	Oryctolagus cuniculus
aeFab98 light chain	L	protein	214	Oryctolagus cuniculus

Sequence of entity 1 (A, B), FASTA

>30AF_1 Isoform 1 of Immunoglobulin heavy constant epsilon (chains A, B)
DIVASRDFTPPTVKILQSSCDGGGHFPPTIQLLCLVSGYTPGTIQITWLEDGQVMDVDLS
TASTTQEGELASTQSELTLSQKHWLSDRTYTCQVTYQGHTFEDSTKKCADSNPRGVSAYL
SRPSPFDLFIRKSPTITCLVVDLAPSKGTVQLTWSRASGKPVNHSTRKEEKQRNGTLTVT
STLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKR
TLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKD
EFICRAVHEAASPSQTVQRAVSVNPGK

Sequence of entity 2 (H), FASTA

>30AF_2 aeFab98 heavy chain (chains H)
QEQLEESGGDLVKPEGSLTLTCTASGFSFSSSYWICWVRQAPGKGLEWIGCIVVSSGSTY
YASWAKGRFTISKTSSTTVTLQMTSLTAADTATYFCARESVGSAYYTFDLWGPGTLVTVS
SGQPKAPSVFPLAPCCGDTPSSTVTLGCLVKGYLPEPVTVTWNSGTLTNGVRTFPSVRQS
SGLYSLSSVVSVTSSSQPVTCNVAHPATNTKVDKTV

Sequence of entity 3 (L), FASTA

>30AF_3 aeFab98 light chain (chains L)
AYDMTQTPASVEVAVGGTVTIKCQASQSISNALSWYQQKPGQRPKLLIYDASKMASGVPS
RFKGSGSGTEFTLTISDLECDDAATYYCQQGYSRSGVDSTFGGGTKVVVKRTPVAPTVLI
FPPAADQVATGTVTIVCVANKYFPDVTVTWEVDGTTQTTGIENSKTPQNSADCTYNLSST
LTLTSTQYNSHKEYTCKVTQGTTSVVQSFNRGDC

Primary citation

Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes. Davies, A.M., Drinkwater, N., Beavil, A.J. et al. Proc Natl Acad Sci U S A (2026) 123:e2613091123-e2613091123. DOI 10.1073/pnas.2613091123 · PubMed

Other PDB entries of the same protein (UniProt P01854 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5MOL 1.75 Å, Human IgE-Fc crystal structure
2WQR 1.9 Å, The high resolution crystal structure of IgE Fc
5MOK 2.0 Å, Crystal structure of human IgE-Fc epsilon 3-4
5MOI 2.2 Å, Crystal structure of human IgE-Fc epsilon 3-4
3H9Y 2.23 Å, Crystal structure of the IgE-Fc3-4 domains
5MOJ 2.26 Å, Crystal structure of IgE-Fc epsilon 3-4
1FP5 2.3 Å, Crystal structure analysis of the human IgE-fc CEPSILON3-CEPSILON4 fragment.
3H9Z 2.45 Å, Crystal structure of the IgE-Fc3-4 domains
5HYS 2.5 Å, Structure of IgE complexed with omalizumab
1O0V 2.6 Å, The crystal structure of IgE Fc reveals an asymmetrically bent conformation
5LGJ 2.6 Å, The crystal structure of IgE fc mutant - P333C
4GT7 2.61 Å, An engineered disulfide bond reversibly traps the IgE-Fc3-4 in a closed, non-receptor…

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