4GT7: Ig epsilon chain C region

An engineered disulfide bond reversibly traps the IgE-Fc3-4 in a closed, non-receptor binding conformation. Determined by X-ray diffraction at 2.61 Å resolution. Released 12 Sept 2012.

Method: X-ray diffraction
Resolution: 2.61 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,082
Mol. weight: 102.36 kDa
Released: 12 Sept 2012

Explore 4GT7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GT7 contains 50 α-helices and 72 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: 12 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	355-363	9	1
α-helix	369-370	2
β-strand	371-376	6	2
α-helix	380-385	6
β-strand	386-391	6	1
β-strand	397-404	8	1
α-helix	407-411	5
β-strand	415-421	7	2
β-strand	429-434	6	2
β-strand	441	1	3
α-helix	442-443	2
β-strand	444-449	6	4
α-helix	450-453	4
β-strand	459-469	11	4
β-strand	470	1	3
β-strand	475-480	6	5
β-strand	483-484	2	5
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	5
β-strand	536-541	6	5

Chains B and D: 13 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	337-341	5	6
α-helix	342-344	3
α-helix	345	1
α-helix	346-350	5
β-strand	355-363	9	6
α-helix	369-370	2
β-strand	371-376	6	7
α-helix	380-385	6
β-strand	386-391	6	6
β-strand	397-404	8	6
α-helix	407-411	5
β-strand	415-421	7	7
α-helix	428	1
β-strand	429-434	6	7
β-strand	441	1	8
α-helix	442-443	2
β-strand	444-449	6	9
α-helix	450-453	4
β-strand	459-469	11	9
β-strand	470	1	8
β-strand	475-480	6	10
β-strand	483-484	2	10
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	9
α-helix	493-495	3
β-strand	496-497	2	9
β-strand	503-512	10	9
α-helix	513-518	6
β-strand	522-527	6	10
β-strand	536-541	6	10

Chain C: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	337-341	5	11
α-helix	342-344	3
α-helix	345	1
α-helix	346-350	5
β-strand	355-363	9	11
α-helix	369-370	2
β-strand	371-376	6	12
α-helix	380-382	3
β-strand	386-391	6	11
β-strand	397-404	8	11
α-helix	407-411	5
β-strand	415-421	7	12
β-strand	429-434	6	12
β-strand	441	1	13
α-helix	442-443	2
β-strand	444-449	6	14
α-helix	450-453	4
β-strand	459-469	11	14
β-strand	470	1	13
β-strand	475-480	6	15
β-strand	483-484	2	15
α-helix	485-486	2
α-helix	487-489	3
β-strand	490-492	3	14
α-helix	493-495	3
β-strand	496-497	2	14
β-strand	503-512	10	14
α-helix	513-518	6
β-strand	522-527	6	15
β-strand	536-541	6	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ig epsilon chain C region	A, B, C, D	protein	221	Homo sapiens	P01854 (AlphaFold model)

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

>4GT7_1 Ig epsilon chain C region (chains A, B, C, D)
ADPAADSNPRCVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNH
STRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPE
VYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFF
VFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNP

Primary citation

An engineered disulfide bond reversibly traps the IgE-Fc3-4 in a closed, nonreceptor binding conformation. Wurzburg, B.A., Kim, B., Tarchevskaya, S.S. et al. J Biol Chem (2012) 287:36251-36257. DOI 10.1074/jbc.M112.407502 · 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.
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

Browse structure collections

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