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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：O60741 New Search
17PDB entries
17Biological assembly
100chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
5U6O Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel Deposited 2016-12-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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
8T4Y Human HCN1 F186C S264C C309A bound to cAMP, reconstituted in LMNG + SPL Deposited 2023-06-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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, C309A Mutation：F186C, S264C, C309A Mutation：F186C, S264C, C309A 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
8T50 Open human HCN1 F186C S264C bound to cAMP, reconstituted in LMNG + SPL Deposited 2023-06-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.