3JAC: Cryo-EM study of a channel

Cryo-EM study of a channel. Determined by electron microscopy at 4.8 Å resolution. Released 23 Sept 2015.

Method: Electron microscopy
Resolution: 4.8 Å
Organism: Mus musculus
Chains: 3
Atoms: 15,741
Mol. weight: 704.5 kDa
Released: 23 Sept 2015

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

Secondary structure: helices and β-sheets

3JAC contains 148 α-helices and 48 β-strands across 3 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: 49 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	202-239	38
α-helix	245-249	5
α-helix	250-254	5
α-helix	255-295	41
α-helix	448-470	23
α-helix	564-575	12
α-helix	878-895	18
α-helix	998-1013	16
α-helix	1014-1018	5
α-helix	1121-1135	15
α-helix	1138-1144	7
α-helix	1249-1262	14
α-helix	1365-1380	16
α-helix	1381-1385	5
α-helix	1488-1504	17
α-helix	1510-1513	4
α-helix	1740-1758	19
α-helix	1760-1779	20
α-helix	1783-1791	9
α-helix	1792-1797	6
α-helix	1798-1803	6
α-helix	1962-1968	7
α-helix	1970-1973	4
α-helix	1976-1988	13
α-helix	1992-2020	29
α-helix	2026-2046	21
α-helix	2056-2077	22
α-helix	2083-2104	22
α-helix	2107-2110	4
α-helix	2112-2122	11
α-helix	2124-2148	25
α-helix	2150-2174	25
α-helix	2176-2179	4
α-helix	2187-2211	25
β-strand	2219	1	1
β-strand	2225-2232	8	2
α-helix	2236-2237	2
β-strand	2239-2243	5	2
β-strand	2248-2250	3	3
α-helix	2251-2252	2
α-helix	2253-2263	11
α-helix	2267-2273	7
α-helix	2278-2280	3
β-strand	2281-2287	7	3
β-strand	2289	1	4
α-helix	2298-2310	13
β-strand	2315-2324	10	2
α-helix	2327-2329	3
β-strand	2335-2344	10	2
α-helix	2349-2357	9
β-strand	2366-2372	7	4
β-strand	2375-2378	4	3
β-strand	2383	1	2
β-strand	2386	1	3
α-helix	2394-2397	4
β-strand	2399-2405	7	4
β-strand	2408	1	5
β-strand	2427	1	5
β-strand	2430-2434	5	4
β-strand	2443-2450	8	3
β-strand	2453	1	1
α-helix	2462-2483	22
α-helix	2487-2496	10
α-helix	2501-2510	10
α-helix	2512-2519	8
α-helix	2522-2524	3
α-helix	2528-2543	16

Chain B: 49 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	202-241	40
α-helix	244-248	5
α-helix	251-295	45
α-helix	448-470	23
α-helix	564-575	12
α-helix	878-895	18
α-helix	998-1013	16
α-helix	1014-1018	5
α-helix	1121-1129	9
α-helix	1131-1146	16
α-helix	1249-1262	14
α-helix	1365-1380	16
α-helix	1381-1385	5
α-helix	1488-1504	17
α-helix	1509-1511	3
α-helix	1740-1758	19
α-helix	1760-1779	20
α-helix	1786-1803	18
α-helix	1962-1968	7
α-helix	1970-1973	4
α-helix	1976-1988	13
α-helix	1995-2020	26
α-helix	2026-2049	24
α-helix	2058-2062	5
α-helix	2063-2077	15
α-helix	2083-2104	22
α-helix	2107-2110	4
α-helix	2112-2122	11
α-helix	2124-2148	25
α-helix	2150-2174	25
α-helix	2176-2179	4
α-helix	2187-2202	16
α-helix	2203-2207	5
α-helix	2208-2211	4
β-strand	2225-2232	8	6
α-helix	2236-2237	2
β-strand	2239-2243	5	6
β-strand	2248-2250	3	7
α-helix	2251-2252	2
α-helix	2253-2263	11
α-helix	2267-2273	7
α-helix	2278-2280	3
β-strand	2281-2287	7	7
β-strand	2289	1	8
α-helix	2298-2310	13
β-strand	2315-2324	10	6
α-helix	2327-2329	3
β-strand	2335-2344	10	6
α-helix	2349-2357	9
β-strand	2366-2372	7	8
β-strand	2375-2378	4	7
β-strand	2383	1	6
β-strand	2386	1	7
α-helix	2394-2397	4
β-strand	2399-2407	9	8
β-strand	2428-2434	7	8
β-strand	2443-2450	8	7
α-helix	2462-2483	22
α-helix	2487-2496	10
α-helix	2501-2510	10
α-helix	2512-2519	8
α-helix	2522-2524	3
α-helix	2528-2543	16

Chain C: 50 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	202-243	42
α-helix	246-248	3
α-helix	249	1
α-helix	250-254	5
α-helix	255-295	41
α-helix	448-470	23
α-helix	564-575	12
α-helix	878-895	18
α-helix	998-1013	16
α-helix	1014-1018	5
α-helix	1121-1140	20
α-helix	1142-1146	5
α-helix	1249-1262	14
α-helix	1365-1380	16
α-helix	1381-1385	5
α-helix	1488-1504	17
α-helix	1509-1511	3
α-helix	1740-1758	19
α-helix	1760-1779	20
α-helix	1783-1803	21
α-helix	1962-1968	7
α-helix	1970-1973	4
α-helix	1976-1982	7
α-helix	1983-1987	5
α-helix	1988-1990	3
α-helix	1996-2020	25
α-helix	2026-2047	22
α-helix	2059-2077	19
α-helix	2083-2104	22
α-helix	2107-2110	4
α-helix	2112-2122	11
α-helix	2124-2148	25
α-helix	2150-2174	25
α-helix	2176-2179	4
α-helix	2187-2211	25
β-strand	2219	1	9
β-strand	2225-2232	8	10
α-helix	2236-2237	2
β-strand	2239-2243	5	10
β-strand	2248-2250	3	11
α-helix	2251-2252	2
α-helix	2253-2263	11
α-helix	2267-2273	7
α-helix	2278-2280	3
β-strand	2281-2287	7	11
β-strand	2289	1	12
α-helix	2298-2310	13
β-strand	2315-2324	10	10
α-helix	2327-2329	3
β-strand	2335-2344	10	10
α-helix	2349-2357	9
β-strand	2366-2372	7	12
β-strand	2375-2378	4	11
β-strand	2383	1	10
β-strand	2386	1	11
α-helix	2394-2397	4
β-strand	2399-2408	10	12
β-strand	2427-2434	8	12
β-strand	2443-2450	8	11
β-strand	2453	1	9
α-helix	2462-2483	22
α-helix	2487-2496	10
α-helix	2501-2510	10
α-helix	2512-2519	8
α-helix	2522-2524	3
α-helix	2528-2543	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Piezo-type mechanosensitive ion channel component 1	A, B, C	protein	2553	Mus musculus	E2JF22 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>3JAC_1 Piezo-type mechanosensitive ion channel component 1 (chains A, B, C)
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XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFFHDILHTKYRAATDVYALM
FLADIVDIIIIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLR
KTVLGKLAFQVVLVVAIHIWMFFILPAVTERMFSQNAVAQLWYFVKCIYFALSAYQIRCG
YPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYA
NIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVV
NQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFISQYSPED
IVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTVEYTNEKH
TLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLG
VRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKVSPPSLGF
LAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELE
LEEELYAKLIFLYRSPETMIKWTRERELEVLFQ

Primary citation

Architecture of the mammalian mechanosensitive Piezo1 channel. Ge, J., Li, W., Zhao, Q. et al. Nature (2015) 527:64-69. DOI 10.1038/nature15247 · PubMed

Other PDB entries of the same protein (UniProt E2JF22 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4RAX 1.45 Å, A regulatory domain of an ion channel
7WLT 3.46 Å, the Curved Structure of mPIEZO1 in Lipid Bilayer
9VED 3.63 Å, The cryo-EM structure of mouse Piezo1-MDFI complex
8IMZ 3.66 Å, Cryo-EM structure of mouse Piezo1-MDFIC complex (composite map)
11YE 3.7 Å, Curved structure of mPiezo1 in plasma membrane vesicles
6B3R 3.8 Å, Structure of the mechanosensitive channel Piezo1
6BPZ 3.8 Å, Structure of the mechanically activated ion channel Piezo1
5Z10 3.97 Å, Structure of the mechanosensitive Piezo1 channel
8IXO 4.0 Å, Intermediate structure of mPIEZO1-S2472E
8IXN 4.07 Å, Curved structure of mPIEZO1-S2472E
6LQI 4.5 Å, Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1
11ZC 6.0 Å, Flat structure of mPiezo1 in plasma membrane vesicles

Browse structure collections

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