1l4w

NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

alpha-Bungarotoxin

OrganismNot specified

UniProt P60615

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Acetylcholine receptor protein × 1 (P02711) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NXL1A_BUNMU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–74; UniProt 1–74

Acetylcholine receptor protein

OrganismNot specified

UniProt P02711

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 alpha-Bungarotoxin × 1 (P60615) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ACHA_TORMA
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–23; UniProt 206–226

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1l4w
Deposition date deposition_date2002-03-06
Structure title titleNMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin
Keywords keywordsprotein-protein complex, intermolecular beta sheet, bungarotoxin, acetylcholine receptor, Receptor, Toxin; Receptor, Toxin
Experimental Method methodSOLUTION NMR
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1l4w__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1l4w__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1l4w__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)15.06 Å
Rg (electron density)13.96 Å
Total Rg15.09 Å
Atom count1498
Residues99
Excluded volume13621 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1l4w__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1l4wa_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.1 — Snake venom toxins

CATH v4.4 (1 domains)

Domain ID domain_id1l4wA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
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7. Citations (1)