3FFQ: HCN2I 443-640 apo-state

HCN2I 443-640 apo-state. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Jun 2009.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,906
Mol. weight: 47.98 kDa
Released: 23 Jun 2009

Explore 3FFQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FFQ contains 24 α-helices and 20 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	446-462	17
α-helix	467-481	15
α-helix	488-494	7
α-helix	497-507	11
α-helix	509-514	6
α-helix	516-518	3
α-helix	523-530	8
β-strand	534-538	5	1
β-strand	543-545	3	2
β-strand	550	1	3
α-helix	551	1
β-strand	553-559	7	1
β-strand	562-565	4	2
β-strand	571-574	4	2
β-strand	579-580	2	1
α-helix	583-587	5
β-strand	590	1	3
β-strand	594-597	4	2
β-strand	601-607	7	1
α-helix	608-617	10
α-helix	619-621	3
α-helix	622-629	8

Chain B: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	444-462	19
α-helix	467-481	15
α-helix	488-492	5
α-helix	497-507	11
α-helix	509-514	6
α-helix	516-518	3
α-helix	523-530	8
β-strand	534-538	5	4
β-strand	543-545	3	5
β-strand	550	1	6
α-helix	551	1
β-strand	553-559	7	4
β-strand	561-565	5	5
β-strand	572-575	4	5
β-strand	579-580	2	4
α-helix	583-587	5
β-strand	590	1	6
β-strand	594-597	4	5
β-strand	601-607	7	4
α-helix	608-617	10
α-helix	619-621	3
α-helix	622-628	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2	A, B	protein	202	Mus musculus	O88703 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3FFQ_1 Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (chains A, B)
GSAMDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGP
LREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQ
HGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEY
PMMRRAFETVAIDRLDRIGKKN

Primary citation

Mapping the structure and conformational movements of proteins with transition metal ion FRET. Taraska, J.W., Puljung, M.C., Olivier, N.B. et al. Nat Methods (2009) 6:532-537. DOI 10.1038/nmeth.1341 · PubMed

Other PDB entries of the same protein (UniProt O88703 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3BPZ 1.65 Å, HCN2-I 443-460 E502K in the presence of cAMP
5KHH 1.77 Å, HCN2 CNBD in complex with inosine-3', 5'-cyclic monophosphate (cIMP)
1Q3E 1.9 Å, HCN2J 443-645 in the presence of cGMP
3ETQ 1.9 Å, X-ray structure of cysteine-free fragment of mHCN2 C-terminal region from amino acids…
1Q43 2.0 Å, HCN2I 443-640 in the presence of cAMP, selenomethionine derivative
5KHJ 2.01 Å, HCN2 CNBD in complex with uridine-3', 5'-cyclic monophosphate (cUMP)
5JON 2.04 Å, Crystal structure of the unliganded form of HCN2 CNBD
5KHK 2.07 Å, HCN2 CNBD in complex with 2-aminopurine riboside-3', 5'-cyclic monophosphate (2-NH2-cPuMP)
5KHI 2.1 Å, HCN2 CNBD in complex with purine riboside-3', 5'-cyclic monophosphate (cPuMP)
5KHG 2.24 Å, HCN2 CNBD in complex with cytidine-3', 5'-cyclic monophosphate (cCMP)
2Q0A 2.25 Å, Structure and rearrangements in the carboxy-terminal region of SpIH channels
1Q5O 2.3 Å, HCN2J 443-645 in the presence of cAMP, selenomethionine derivative

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