2BJM: SPE7:Anthrone Complex

SPE7:Anthrone Complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 18 Aug 2005.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: MUS MUSCULUS
Chains: 2
Atoms: 1,782
Mol. weight: 25.3 kDa
Ligands: ANF
Released: 18 Aug 2005

Explore 2BJM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BJM contains 3 α-helices and 20 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: 1 helix, 9 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
β-strand	9-12	4	2
β-strand	18-25	8	1
β-strand	35-40	6	2
β-strand	44-47	4	2
β-strand	68-73	6	1
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-97	6	2
β-strand	114-118	5	2

Chain L: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	3
β-strand	9-12	4	4
β-strand	18-24	7	3
β-strand	36-41	6	4
β-strand	45-51	7	4
β-strand	55-56	2	4
α-helix	57	1
β-strand	64-69	6	3
β-strand	72-77	6	3
α-helix	82-84	3
β-strand	87-93	7	4
β-strand	98-100	3	4
β-strand	104-108	5	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
IgE SPE7 heavy chain	H	protein	120	MUS MUSCULUS
IgE SPE7 light chain	L	protein	110	MUS MUSCULUS	P01724 (AlphaFold model)

Sequence of entity 1 (H), FASTA

>2BJM_1 IGE SPE7 HEAVY CHAIN (chains H)
EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKY
NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSS

Sequence of entity 2 (L), FASTA

>2BJM_2 IGE SPE7 LIGHT CHAIN (chains L)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGV
PARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLE

Ligands and cofactors

ID	Name	Formula	Copies
ANF	Anthrone	C14 H10 O	1

Primary citation

Structure and Kinetics of a Transient Antibody Binding Intermediate Reveal a Kinetic Discrimination Mechanism in Antigen Recognition. James, L.C., Tawfik, D.S. Proc Natl Acad Sci U S A (2005) 102:12730. DOI 10.1073/PNAS.0500909102 · 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
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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