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8t4y

Human HCN1 F186C S264C C309A bound to cAMP, reconstituted in LMNG + SPL

Method: ELECTRON MICROSCOPY Dmax: 134.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1

Homo sapiens

UniProt O60741

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–890 Chain B； UniProt 1–890 Chain C； UniProt 1–890 Chain D； UniProt 1–890 Mutation：F186C, S264C, C309A CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.58 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.

Other PDB Difference from Current Entry 8T4Y Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5U6O Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel Deposited 2016-12-08 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain A 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain B 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain B 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain C 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain C 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain D 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain D 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
5U6P Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP Deposited 2016-12-08 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain A 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain B 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain B 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain C 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain C 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain D 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain D 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Not recorded CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.51 Å
6UQF Human HCN1 channel in a hyperpolarized conformation Deposited 2019-10-19 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa）
Chain A 866–890（25 aa）
Chain B 1–635（635 aa）
Chain B 866–890（25 aa）
Chain C 1–635（635 aa）
Chain C 866–890（25 aa）
Chain D 1–635（635 aa）
Chain D 866–890（25 aa）
Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 HG MERCURY (II) ION × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.04 Å
6UQG Human HCN1 channel Y289D mutant Deposited 2019-10-19 Different construct Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa）
Chain A 866–890（25 aa）
Chain B 1–635（635 aa）
Chain B 866–890（25 aa）
Chain C 1–635（635 aa）
Chain C 866–890（25 aa）
Chain D 1–635（635 aa）
Chain D 866–890（25 aa）
Mutation：Y289D Mutation：Y289D Mutation：Y289D Mutation：Y289D Mutation：Y289D Mutation：Y289D Mutation：Y289D Mutation：Y289D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.54 Å
8T4M Closed human HCN1 F186C S264C bound to cAMP, reconstituted in LMNG + SPL Deposited 2023-06-09 Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–890（890 aa）
Chain B 1–890（890 aa）
Chain C 1–890（890 aa）
Chain D 1–890（890 aa）
Mutation：F186C S264C Mutation：F186C S264C Mutation：F186C S264C Mutation：F186C S264C CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.16 Å
8T50 Open human HCN1 F186C S264C bound to cAMP, reconstituted in LMNG + SPL Deposited 2023-06-12 Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–890（890 aa）
Chain B 1–890（890 aa）
Chain C 1–890（890 aa）
Chain D 1–890（890 aa）
Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C Mutation：F186C, S264C CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
8UC7 HCN1 complex with propofol Deposited 2023-09-25 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain A 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain B 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain B 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain C 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain C 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain D 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain D 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Not recorded PFL 2,6-BIS(1-METHYLETHYL)PHENOL × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8UC8 HCN1 nanodisc Deposited 2023-09-25 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain A 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain B 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain B 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain C 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain C 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Chain D 1–635（635 aa） Fragment：UNP residues 1-635,866-890
Chain D 866–890（25 aa） Fragment：UNP residues 1-635,866-890
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8Y60 Structural mechanism of human HCN1 hyperpolarization-activated channel inhibition by ivabradine Deposited 2024-02-01 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–890（890 aa）
Chain B 1–890（890 aa）
Chain C 1–890（890 aa）
Chain D 1–890（890 aa）
Not recorded CLR CHOLESTEROL × 4 VNZ Ivabradine × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.23 Å
9BC6 HCN1 M305L with propofol Deposited 2024-04-07 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa）
Chain A 866–890（25 aa）
Chain B 1–635（635 aa）
Chain B 866–890（25 aa）
Chain C 1–635（635 aa）
Chain C 866–890（25 aa）
Chain D 1–635（635 aa）
Chain D 866–890（25 aa）
Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 8 PFL 2,6-BIS(1-METHYLETHYL)PHENOL × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
9BC7 HCN1 M305L holo Deposited 2024-04-08 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–635（635 aa）
Chain A 866–890（25 aa）
Chain B 1–635（635 aa）
Chain B 866–890（25 aa）
Chain C 1–635（635 aa）
Chain C 866–890（25 aa）
Chain D 1–635（635 aa）
Chain D 866–890（25 aa）
Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L Mutation：M305L PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 12 CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9PXN Human apo HCN1 nanodisc Deposited 2025-08-06 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–635（634 aa）
Chain B 2–635（634 aa）
Chain C 2–635（634 aa）
Chain D 2–635（634 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
9R1T Structure of the human chimera HCN112 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP. Deposited 2025-04-28 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–401（401 aa）
Chain B 1–401（401 aa）
Chain C 1–401（401 aa）
Chain D 1–401（401 aa）
Not recorded CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.34 Å
9R1U Structure of the human HCN1dC hyperpolarization-activated cyclic nucleotide-gated ion channel. Deposited 2025-04-28 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–401（401 aa）
Chain B 1–401（401 aa）
Chain C 1–401（401 aa）
Chain D 1–401（401 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.92 Å
9R1V Structure of the human chimera HCN112 hyperpolarization-activated cyclic nucleotide-gated ion channel. Deposited 2025-04-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–401（401 aa）
Chain B 1–401（401 aa）
Chain C 1–401（401 aa）
Chain D 1–401（401 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.53 Å
9Z6T Human HCN1 in complex with cAMP in nanodisc Deposited 2025-11-14 Different construct Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–635（634 aa）
Chain B 2–635（634 aa）
Chain C 2–635（634 aa）
Chain D 2–635（634 aa）
Not recorded CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HCN1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–890； UniProt 1–890 Author chain B； PDBConstruct 1–890； UniProt 1–890 Author chain C； PDBConstruct 1–890； UniProt 1–890 Author chain D； PDBConstruct 1–890； UniProt 1–890

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 8t4y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t4y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t4y
Deposition date deposition_date2023-06-12
Structure title titleHuman HCN1 F186C S264C C309A bound to cAMP, reconstituted in LMNG + SPL
Keywords keywordsMembrane Protein, Ion Channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier42.24 Å
Radius of gyration Rg (electron density) rg_electron41.30 Å
Forward intensity I(0) i0590965000.00
Molecular weight molecular_weight188410.0 kDa
Excluded volume excluded_volume230470 ų
Envelope volume envelope_volume374140 ų
Hydration-shell volume shell_volume74088 ų
Envelope diameter envelope_diameter134.7 Å
Shell Rg shell_rg48.45 Å
Envelope Rg envelope_rg40.34 Å
Shape Rg shape_rg41.38 Å
Total Rg total_rg41.42 Å
Total atoms total_atoms13348
Residues n_residues2004
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax134.2 Å
Rg (real space) rg_real42.05 Å
Rg uncertainty (real space) rg_real_error0.99 Å
I(0) (real space) i0_real5.9100e+08
I(0) uncertainty (real space) i0_real_error9.0900e+06
Rg (reciprocal space) rg_reciprocal42.24 Å
I(0) (reciprocal space) i0_reciprocal591100000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.4 Å
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.1850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha56790000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.918
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)