1A6U: B1-8 fv fragment

B1-8 fv fragment. Determined by X-ray diffraction at 2.1 Å resolution. Released 27 May 1998.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,892
Mol. weight: 24.82 kDa
Released: 27 May 1998

Explore 1A6U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1A6U contains 6 α-helices and 23 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, 11 β-strands

Element	Residues	Length	Sheet
β-strand	303-305	3	3
β-strand	309-312	4	4
β-strand	318-325	8	3
α-helix	329-331	3
β-strand	333-339	7	4
β-strand	345-351	7	4
β-strand	358-360	3	4
α-helix	362-364	3
β-strand	368-373	6	3
β-strand	378-383	6	3
α-helix	388-390	3
β-strand	392-399	8	4
β-strand	407-410	4	4
β-strand	414-418	5	4

Chain L: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	1
β-strand	9-12	4	2
β-strand	18-24	7	1
β-strand	27	1	1
α-helix	31-33	3
β-strand	36-41	6	2
β-strand	45-51	7	2
β-strand	55-56	2	2
α-helix	57	1
β-strand	64-69	6	1
β-strand	72-77	6	1
α-helix	82-84	3
β-strand	86-93	8	2
β-strand	98-100	3	2
β-strand	104-108	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
B1-8 fv (light chain)	L	protein	108	Mus musculus	P01724 (AlphaFold model)
B1-8 fv (heavy chain)	H	protein	120	Mus musculus	P01751

Sequence of entity 1 (L), FASTA

>1A6U_1 B1-8 FV (LIGHT CHAIN) (chains L)
AVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGVP
ARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVL

Sequence of entity 2 (H), FASTA

>1A6U_2 B1-8 FV (HEAVY CHAIN) (chains H)
QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKY
NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARYDYYGSSYFDYWGQGTTVTVSS

Primary citation

X-Ray Structures of Fv Fragment and its (4-Hydroxy-3-Nitrophenyl)Acetate Complex of Murine B1-8 Antibody. Simon, T., Henrick, K., Hirshberg, M. et al. To be published.

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
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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