1DL7: Protein)

The structural basis of repertoire shift in an immune response to phosphocholine. Determined by X-ray diffraction at 2.35 Å resolution. Released 13 Dec 2000.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,779
Mol. weight: 24.18 kDa
Ligands: NCH
Released: 13 Dec 2000

Explore 1DL7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DL7 contains 3 α-helices and 22 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: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	4
β-strand	18-23	6	4
β-strand	34-39	6	5
β-strand	46-51	6	5
β-strand	57-59	3	5
α-helix	61-63	3
β-strand	70-72	3	4
β-strand	77-82	6	4
α-helix	87-89	3
β-strand	91-97	7	5
β-strand	102	1	5
β-strand	108-109	2	5

Chain L: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	1
β-strand	9-12	4	2
β-strand	17-20	4	3
β-strand	23-24	2	1
β-strand	36-41	6	2
β-strand	45-51	7	2
β-strand	55-56	2	2
β-strand	64-69	6	3
β-strand	72-78	7	3
α-helix	82-84	3
β-strand	86-92	7	2
β-strand	99-100	2	2
β-strand	104-108	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (antibody M3C65 (light chain))	L	protein	109	Mus musculus	P01724 (AlphaFold model)
Protein (antibody M3C65 (heavy chain))	H	protein	112	Mus musculus	P01820 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1DL7_1 PROTEIN (ANTIBODY M3C65 (LIGHT CHAIN)) (chains L)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTKHRTPGA
PARFSGSLIGDKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVL

Sequence of entity 2 (H), FASTA

>1DL7_2 PROTEIN (ANTIBODY M3C65 (HEAVY CHAIN)) (chains H)
QVQLKESGPGLVAPSQSLSITCTVSGFSLTGYGVNWVRQPPGKGLEWLGMIWGDGSTDYN
SALKSRLNISKDKSKSQVFLRMYSLQTDDTARYYCARDYGPYWGQGTLVTVS

Ligands and cofactors

ID	Name	Formula	Copies
NCH	P-nitrophenyl-phosphocholine	C11 H18 N2 O6 P	1

Primary citation

The structural basis of repertoire shift in an immune response to phosphocholine. Brown, M., Schumacher, M.A., Wiens, G.D. et al. J Exp Med (2000) 191:2101-2112. DOI 10.1084/jem.191.12.2101 · 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
1OAR 2.23 Å, Fv IgE SPE-7 in complex with Alizarin Red
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 1DL7 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.