1OAR: Fv IgE SPE-7

Fv IgE SPE-7 in complex with Alizarin Red. Determined by X-ray diffraction at 2.23 Å resolution. Released 15 Jan 2004.

Method: X-ray diffraction
Resolution: 2.23 Å
Organism: MUS MUSCULUS
Chains: 8
Atoms: 7,050
Mol. weight: 104.85 kDa
Ligands: CAC, AZN
Released: 15 Jan 2004

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

Secondary structure: helices and β-sheets

1OAR contains 20 α-helices and 92 β-strands across 8 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: 4 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
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

Chain I: 0 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	18-23	6	4
β-strand	33-39	7	5
β-strand	46-51	6	5
β-strand	58-60	3	5
β-strand	68-71	4	4
β-strand	78-83	6	4
β-strand	93-100	8	5
β-strand	106-108	3	5
β-strand	109	1	6
β-strand	110	1	5
β-strand	114-115	2	5

Chain K: 0 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	18-22	5	10
β-strand	33-39	7	11
β-strand	46-51	6	11
β-strand	58-60	3	11
β-strand	68-71	4	10
β-strand	79-83	5	10
β-strand	93-100	8	11
β-strand	106-110	5	11
β-strand	114-115	2	11

Chains L and N: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	12
β-strand	9-12	4	3
β-strand	17-24	8	12
β-strand	27	1	12
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	12
β-strand	72-78	7	12
α-helix	82-84	3
β-strand	86-94	9	3
β-strand	97-100	4	3
β-strand	104-108	5	3

Chain M: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	13
β-strand	9-12	4	6
β-strand	17-22	6	13
α-helix	31-33	3
β-strand	36-41	6	6
β-strand	45-51	7	6
β-strand	55-56	2	6
α-helix	57	1
β-strand	64-69	6	13
β-strand	72-78	7	13
α-helix	82-84	3
β-strand	86-94	9	6
β-strand	97-100	4	6
β-strand	104-108	5	6

Chain O: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	15
β-strand	9-12	4	16
β-strand	17-24	8	15
α-helix	31-33	3
β-strand	36-41	6	16
β-strand	45-51	7	16
β-strand	55-56	2	16
α-helix	57	1
β-strand	64-69	6	15
β-strand	72-78	7	15
α-helix	82-84	3
β-strand	86-94	9	16
β-strand	97-100	4	16
β-strand	104-108	5	16

Molecules and chains

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

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

>1OAR_1 IMMUNOGLOBULIN E (chains H, I, J, K)
EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKY
NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSS
AA

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

>1OAR_2 IMMUNOGLOBULING E (chains L, M, N, O)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGV
PARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLT

Ligands and cofactors

ID	Name	Formula	Copies
CAC	Cacodylate ion	C2 H6 As O2	2
AZN	Alizarin red	C14 H8 O7 S	4

Water and common crystallization additives (DMS, EDO, NA, CL) 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
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
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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