9upf

Cryo-EM structure of human olfactory CNG channel in cAMP-bound open state

Method: ELECTRON MICROSCOPY Dmax: 124.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cyclic nucleotide-gated channel beta-1

Homo sapiens

UniProt Q14028

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–1251 Not recorded Cyclic nucleotide-gated channel alpha-2 × 2 (Q16280) Cyclic nucleotide-gated channel alpha-4 × 1 (Q8IV77) CA CALCIUM ION × 2 CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNGB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–1251; UniProt 1–1251

Cyclic nucleotide-gated channel alpha-2

Homo sapiens

UniProt Q16280

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–664 Chain C; UniProt 1–664 Not recorded Cyclic nucleotide-gated channel beta-1 × 1 (Q14028) Cyclic nucleotide-gated channel alpha-4 × 1 (Q8IV77) CA CALCIUM ION × 2 CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNGA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–664; UniProt 1–664 Author chain C; PDBConstruct 1–664; UniProt 1–664

Cyclic nucleotide-gated channel alpha-4

Homo sapiens

UniProt Q8IV77

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–575 Not recorded Cyclic nucleotide-gated channel beta-1 × 1 (Q14028) Cyclic nucleotide-gated channel alpha-2 × 2 (Q16280) CA CALCIUM ION × 2 CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.59 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNGA4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–575; UniProt 1–575

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9upf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9upf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9upf
Deposition date deposition_date2025-04-28
Structure title titleCryo-EM structure of human olfactory CNG channel in cAMP-bound open state
Keywords keywordsIon Channels, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier40.60
Radius of gyration Rg (electron density) rg_electron39.90
Forward intensity I(0) i0567905000.00
Molecular weight molecular_weight206810.0 kDa
Excluded volume excluded_volume263570 ų
Envelope volume envelope_volume368320 ų
Hydration-shell volume shell_volume74350 ų
Envelope diameter envelope_diameter125.6
Shell Rg shell_rg48.05
Envelope Rg envelope_rg38.83
Shape Rg shape_rg39.89
Total Rg total_rg40.40
Total atoms total_atoms14581
Residues n_residues1774
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax124.0
Rg (real space) rg_real40.35
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real5.6790e+08
I(0) uncertainty (real space) i0_real_error9.0480e+06
Rg (reciprocal space) rg_reciprocal40.60
I(0) (reciprocal space) i0_reciprocal568000000.0000
Solution quality estimate total_estimate0.8944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.0
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.495
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49290000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)