1OAQ: Free conformation Ab1 of the IgE SPE-7

Free conformation Ab1 of the IgE SPE-7. Determined by X-ray diffraction at 1.5 Å resolution. Released 15 Jan 2004.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: MUS MUSCULUS
Chains: 2
Atoms: 2,037
Mol. weight: 26.13 kDa
Released: 15 Jan 2004

Explore 1OAQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OAQ contains 6 α-helices and 25 β-strands across 2 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 H: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
β-strand	10-12	3	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	32-39	8	2
β-strand	45-51	7	2
β-strand	58-60	3	2
α-helix	62-64	3
β-strand	68-73	6	1
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-100	9	2
β-strand	107-108	2	2
β-strand	109	1	3
β-strand	110	1	2
β-strand	114-118	5	2

Chain L: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	4
β-strand	9-12	4	3
β-strand	17-24	8	4
β-strand	27	1	4
α-helix	31-33	3
β-strand	36-41	6	3
β-strand	45-51	7	3
β-strand	55-56	2	3
α-helix	57	1
β-strand	64-69	6	4
β-strand	72-78	7	4
α-helix	82-84	3
β-strand	86-94	9	3
β-strand	97-100	4	3
β-strand	104-108	5	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heavy chain	H	protein	121	MUS MUSCULUS
Light chain	L	protein	120	MUS MUSCULUS	P01724 (AlphaFold model)

Sequence of entity 1 (H), FASTA

>1OAQ_1 HEAVY CHAIN (chains H)
EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKY
NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSS
A

Sequence of entity 2 (L), FASTA

>1OAQ_2 LIGHT CHAIN (chains L)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGV
PARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLGQPKSSPSVTL

Primary citation

Antibody Multispecificity Mediated by Conformational Diversity. James, L.C., Roversi, P., Tawfik, D. Science (2003) 299:1362. DOI 10.1126/SCIENCE.1079731 · PubMed

Other PDB entries of the same protein (UniProt P01724 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1A6V 1.8 Å, B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound
1OAU 1.8 Å, Fv Structure of the IgE SPE-7 in complex with DNP-Ser (immunising hapten)
1A6W 2.0 Å, B1-8 fv fragment complexed with a (4-hydroxy-5-iodo-3-nitrophenyl) acetate compound
1OCW 2.0 Å, Free conformation Ab2 of the IgE SPE-7
1Q0Y 2.0 Å, Anti-Morphine Antibody 9B1 Complexed with Morphine
1A6U 2.1 Å, B1-8 fv fragment
2BJM 2.15 Å, SPE7:Anthrone Complex
1OAR 2.23 Å, Fv IgE SPE-7 in complex with Alizarin Red
1DL7 2.35 Å, The structural basis of repertoire shift in an immune response to phosphocholine
1OAY 2.66 Å, Antibody multispecificity mediated by conformational diversity
1OAX 2.67 Å, Fv Structure of the IgE SPE-7 in complex with acenaphthenequinone
1OAZ 2.78 Å, IgE Fv SPE7 complexed with a recombinant thioredoxin

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