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8ci2

human alpha7 nicotinic receptor in complex with the C4 nanobody under sub-saturating conditions

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Neuronal acetylcholine receptor subunit alpha-7

Homo sapiens

UniProt P36544

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Other combination Heteromer Protein 8 其他Polymer 5 Nanobody C4 × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
2maw

1 assemblies

Homodimer

None

Homotetramer

None

Other homooligomers
7rpm 8f4v

2 assemblies

Heteromeric or nucleic-acid complex
7eki 7ekp 7ekt 7koo 7koq 7kox 8c9x 8cau 8ce4 8ci1 8ci2 8p1h

42 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name ACHA7_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–324； UniProt 24–347 Author chain A； PDBConstruct 328–375； UniProt 455–502 Author chain B； PDBConstruct 1–324； UniProt 24–347 Author chain B； PDBConstruct 328–375； UniProt 455–502 Author chain C； PDBConstruct 1–324； UniProt 24–347 Author chain C； PDBConstruct 328–375； UniProt 455–502 Author chain D； PDBConstruct 1–324； UniProt 24–347 Author chain D； PDBConstruct 328–375； UniProt 455–502 Author chain E； PDBConstruct 1–324； UniProt 24–347 Author chain E； PDBConstruct 328–375； UniProt 455–502

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_id8ci2
Deposition date deposition_date2023-02-08
Structure title titlehuman alpha7 nicotinic receptor in complex with the C4 nanobody under sub-saturating conditions
Keywords keywordsion channel nanobody Nicotinic acetylcholine receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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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.

8ci2__assembly_1__model_1

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

Download this curve (.dat)

8ci2__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8ci2__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）36.92 Å
Rg (electron density)35.79 Å
Total Rg36.59 Å
Atom count21802
Residues1393
Excluded volume198700 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8ci2__assembly_1__model_1 octameric （8） 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 (4)

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7. Citations (1)