5MOK: Human IgE-Fc epsilon 3-4

Crystal structure of human IgE-Fc epsilon 3-4. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Jan 2018.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,173
Mol. weight: 104.13 kDa
Released: 10 Jan 2018

Explore 5MOK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MOK contains 42 α-helices and 78 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: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	337-340	4	1
α-helix	341-344	4
α-helix	345	1
α-helix	346-350	5
β-strand	355-362	8	1
α-helix	365-366	2
β-strand	371-376	6	2
β-strand	386-391	6	1
β-strand	397-404	8	1
α-helix	407-411	5
β-strand	416-421	6	2
β-strand	429-433	5	2
β-strand	441	1	3
α-helix	442-443	2
β-strand	444-449	6	4
α-helix	450-452	3
β-strand	453	1	5
β-strand	456	1	5
β-strand	459-469	11	4
β-strand	470	1	3
β-strand	475-480	6	6
β-strand	483-484	2	6
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	4
α-helix	493-495	3
β-strand	496-497	2	4
β-strand	503-512	10	4
α-helix	513-518	6
β-strand	522-527	6	6
β-strand	536-541	6	6

Chain B: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	337-340	4	7
α-helix	341-344	4
α-helix	345	1
α-helix	346-350	5
β-strand	355-361	7	7
β-strand	371-376	6	8
β-strand	386-391	6	7
β-strand	397-404	8	7
α-helix	407-411	5
β-strand	416-421	6	8
β-strand	429-433	5	8
β-strand	441	1	9
α-helix	442-443	2
β-strand	444-449	6	10
α-helix	450-452	3
β-strand	453	1	11
β-strand	456	1	11
β-strand	459-469	11	10
β-strand	470	1	9
β-strand	475-480	6	12
β-strand	483-484	2	12
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	10
α-helix	493-495	3
β-strand	496-497	2	10
β-strand	503-512	10	10
α-helix	513-518	6
β-strand	522-527	6	12
β-strand	536-541	6	12

Chain C: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	337-340	4	13
α-helix	342-344	3
α-helix	345	1
α-helix	346-350	5
β-strand	355-361	7	13
β-strand	372-376	5	14
α-helix	380-382	3
β-strand	386-391	6	13
β-strand	397-404	8	13
α-helix	407-411	5
β-strand	416-420	5	14
β-strand	429-433	5	14
β-strand	441	1	15
α-helix	442-443	2
β-strand	444-449	6	16
α-helix	450-452	3
β-strand	453	1	17
β-strand	456	1	17
β-strand	459-469	11	16
β-strand	470	1	15
β-strand	475-480	6	18
β-strand	483-484	2	18
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	16
α-helix	493-495	3
β-strand	496-497	2	16
β-strand	503-512	10	16
α-helix	513-518	6
β-strand	522-527	6	18
β-strand	536-541	6	18

Chain D: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	337-341	5	1
α-helix	342-344	3
α-helix	345	1
α-helix	346-350	5
β-strand	355-361	7	1
β-strand	371-376	6	19
β-strand	386-391	6	1
β-strand	397-404	8	1
α-helix	407-411	5
β-strand	416-421	6	19
β-strand	429-433	5	19
β-strand	441	1	20
α-helix	442-443	2
β-strand	444-449	6	21
α-helix	450-453	4
β-strand	459-469	11	21
β-strand	470	1	20
β-strand	475-480	6	22
β-strand	483-484	2	22
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	21
α-helix	493-495	3
β-strand	496-497	2	21
β-strand	503-512	10	21
α-helix	513-518	6
β-strand	522-527	6	22
β-strand	536-541	6	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ig epsilon chain C region	A, B, C, D	protein	223	Homo sapiens	P01854 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5MOK_1 Ig epsilon chain C region (chains A, B, C, D)
ADPCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVQLTWSRASGKPVQH
STRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPE
VYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFF
VFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGK

Primary citation

Thermal sensitivity and flexibility of the C epsilon 3 domains in immunoglobulin E. Dore, K.A., Davies, A.M., Drinkwater, N. et al. Biochim Biophys Acta (2017) 1865:1336-1347. DOI 10.1016/j.bbapap.2017.08.005 · 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
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.
30AF 2.4 Å, Complex between IgE-Fc and anti-IgE Fab aeFab98
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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