1OAU: Fv Structure of the IgE SPE-7

Fv Structure of the IgE SPE-7 in complex with DNP-Ser (immunising hapten). Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Jan 2004.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: MUS MUSCULUS
Chains: 8
Atoms: 5,621
Mol. weight: 101.59 kDa
Ligands: SER, DNF
Released: 15 Jan 2004

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

Secondary structure: helices and β-sheets

1OAU contains 21 α-helices and 65 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.

Chains H and J: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
α-helix	7-9	3
β-strand	10-12	3	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	33-39	7	2
β-strand	45-52	8	2
β-strand	57-60	4	2
α-helix	62-64	3
β-strand	68-73	6	1
α-helix	74-76	3
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-100	9	2
β-strand	106-108	3	2
β-strand	109	1	3
β-strand	110	1	2
β-strand	114-118	5	2

Chains L and N: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	7
β-strand	9-12	4	3
β-strand	17-24	8	7
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	7
β-strand	72-78	7	7
α-helix	82-84	3
β-strand	86-93	8	3
β-strand	98-100	3	3
β-strand	104-108	5	3

Chain M: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	9-12	4	8
β-strand	17-22	6	9
α-helix	31-33	3
β-strand	38-41	4	8
β-strand	45-48	4	8
β-strand	64-69	6	9
β-strand	72-78	7	9
α-helix	82-84	3
β-strand	86-89	4	8
β-strand	104-108	5	8

Chain O: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	9-12	4	11
β-strand	17-23	7	12
α-helix	31-33	3
β-strand	37-41	5	11
β-strand	45-51	7	11
β-strand	55-56	2	11
α-helix	57	1
β-strand	64-69	6	12
β-strand	72-78	7	12
α-helix	82-84	3
β-strand	86-89	4	11
β-strand	104-108	5	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Immunoglobulin E	H, I, J, K	protein	122	MUS MUSCULUS
Immunoglobulin E	L, M, N, O	protein	110	MUS MUSCULUS	P01724 (AlphaFold model)

Sequence of entity 1 (H, I, J, K), FASTA

>1OAU_1 IMMUNOGLOBULIN E (chains H, I, J, K)
EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKY
NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSS
AA

Sequence of entity 2 (L, M, N, O), FASTA

>1OAU_2 IMMUNOGLOBULIN E (chains L, M, N, O)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGV
PARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLT

Ligands and cofactors

ID	Name	Formula	Copies
SER	Serine	C3 H7 N O3	2
DNF	2,4-dinitrophenol	C6 H4 N2 O5	2

Water and common crystallization additives (IMD) are not listed.

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:

1OAQ 1.5 Å, Free conformation Ab1 of the IgE SPE-7
1A6V 1.8 Å, B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound
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

Browse structure collections

About this viewer

MolViewer shows 1OAU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.