Curved structure of mPiezo1 in plasma membrane vesicles. Determined by electron microscopy at 3.7 Å resolution. Released 29 Apr 2026.
Explore 11YE in 3D Show helices and sheets RCSB PDB PDBe
11YE contains 210 α-helices and 42 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 785-824 | 40 | |
| α-helix | 826-839 | 14 | |
| α-helix | 847-864 | 18 | |
| α-helix | 900-903 | 4 | |
| α-helix | 923-950 | 28 | |
| α-helix | 976-983 | 8 | |
| α-helix | 990-997 | 8 | |
| α-helix | 1001-1003 | 3 | |
| α-helix | 1006-1015 | 10 | |
| α-helix | 1016-1020 | 5 | |
| α-helix | 1021-1023 | 3 | |
| α-helix | 1026-1051 | 26 | |
| α-helix | 1073-1080 | 8 | |
| α-helix | 1088-1090 | 3 | |
| α-helix | 1092-1112 | 21 | |
| α-helix | 1142-1144 | 3 | |
| α-helix | 1149-1176 | 28 | |
| α-helix | 1179-1201 | 23 | |
| α-helix | 1205-1230 | 26 | |
| α-helix | 1231-1233 | 3 | |
| α-helix | 1243-1248 | 6 | |
| α-helix | 1263-1267 | 5 | |
| α-helix | 1280-1291 | 12 | |
| α-helix | 1292-1295 | 4 | |
| α-helix | 1296-1299 | 4 | |
| α-helix | 1303-1364 | 62 | |
| α-helix | 1404-1407 | 4 | |
| α-helix | 1413-1415 | 3 | |
| α-helix | 1418-1420 | 3 | |
| α-helix | 1497-1523 | 27 | |
| α-helix | 1525-1547 | 23 | |
| α-helix | 1553-1558 | 6 | |
| α-helix | 1657-1669 | 13 | |
| α-helix | 1672-1685 | 14 | |
| α-helix | 1687-1699 | 13 | |
| α-helix | 1706-1713 | 8 | |
| α-helix | 1714-1718 | 5 | |
| α-helix | 1726-1747 | 22 | |
| α-helix | 1753-1755 | 3 | |
| α-helix | 1758-1761 | 4 | |
| α-helix | 1770-1774 | 5 | |
| α-helix | 1786-1803 | 18 | |
| α-helix | 1947-1967 | 21 | |
| α-helix | 1977-1996 | 20 | |
| α-helix | 2016-2039 | 24 | |
| α-helix | 2043-2059 | 17 | |
| α-helix | 2060-2064 | 5 | |
| α-helix | 2065-2068 | 4 | |
| α-helix | 2077-2098 | 22 | |
| α-helix | 2117-2127 | 11 | |
| α-helix | 2131-2143 | 13 | |
| α-helix | 2151-2174 | 24 | |
| α-helix | 2181-2184 | 4 | |
| α-helix | 2185-2214 | 30 | |
| β-strand | 2219 | 1 | 1 |
| β-strand | 2226-2232 | 7 | 2 |
| β-strand | 2240-2243 | 4 | 2 |
| α-helix | 2245-2247 | 3 | |
| β-strand | 2248-2250 | 3 | 3 |
| α-helix | 2252-2262 | 11 | |
| α-helix | 2267-2274 | 8 | |
| β-strand | 2281-2287 | 7 | 3 |
| α-helix | 2291-2294 | 4 | |
| α-helix | 2298-2310 | 13 | |
| α-helix | 2314 | 1 | |
| β-strand | 2315-2324 | 10 | 2 |
| α-helix | 2327-2329 | 3 | |
| β-strand | 2335-2344 | 10 | 2 |
| α-helix | 2349-2358 | 10 | |
| β-strand | 2366-2372 | 7 | 4 |
| β-strand | 2375-2378 | 4 | 3 |
| α-helix | 2385 | 1 | |
| β-strand | 2386 | 1 | 3 |
| α-helix | 2387 | 1 | |
| β-strand | 2399-2409 | 11 | 4 |
| β-strand | 2426-2434 | 9 | 4 |
| β-strand | 2443-2450 | 8 | 3 |
| β-strand | 2453 | 1 | 1 |
| α-helix | 2466-2485 | 20 | |
| α-helix | 2489-2491 | 3 | |
| α-helix | 2492-2495 | 4 | |
| α-helix | 2501-2515 | 15 | |
| α-helix | 2519-2532 | 14 | |
| α-helix | 2536-2542 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Piezo-type mechanosensitive ion channel component 1 | C, D, E | protein | 2561 | Mus musculus | E2JF22 (AlphaFold model) |
>11YE_1 Piezo-type mechanosensitive ion channel component 1 (chains C, D, E) MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLL RALLCLSLLFLVAHLAFQICLHTVPHLDQFLGQNGSLWVKVSQHIGVTRLDLKDIFNTTR LVAPDLGVLLASSLCLGLCGRLTRKAGQSRRTQELQDDDDDDDDDDEDIDAAPAVGLKGA PALATKRRLWLASRFRVTAHWLLMTSGRTLVIVLLALAGIAHPSAFSSIYLVVFLAICTW WSCHFPLSPLGFNTLCVMVSCFGAGHLICLYCYQTPFIQDMLPPGNIWARLFGLKNFVDL PNYSSPNALVLNTKHAWPIYVSPGILLLLYYTATSLLKLHKSCPSELRKETPREDEEHEL ELDHLEPEPQARDATQGEMPMTTEPDLDNCTVHVLTSQSPVRQRPVRPRLAELKEMSPLH GLGHLIMDQSYVCALIAMMVWSIMYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLY GLTLCCLRYVWAMELPELPTTLGPVSLHQLGLEHTRYPCLDLGAMLLYLLTFWLLLRQFV KEKLLKKQKVPAALLEVTVADTEPTQTQTLLRSLGELVTGIYVKYWIYVCAGMFIVVSFA GRLVVYKIVYMFLFLLCLTLFQVYYTLWRKLLRVFWWLVVAYTMLVLIAVYTFQFQDFPT YWRNLTGFTDEQLGDLGLEQFSVSELFSSILIPGFFLLACILQLHYFHRPFMQLTDLEHV PPPGTRHPRWAHRQDAVSEAPLLEHQEEEEVFREDGQSMDGPHQATQVPEGTASKWGLVA DRLLDLAASFSAVLTRIQVFVRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFAL PYPRFRPMASCLSTVWTCIIIVCKMLYQLKIVNPHEYSSNCTEPFPNNTNLQPLEINQSL LYRGPVDPANWFGVRKGYPNLGYIQNHLQILLLLVFEAVVYRRQEHYRRQHQQAPLPAQA VCADGTRQRLDQDLLSCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFMVILHGCWLVAI LTRRRREAIARLWPNYCLFLTLFLLYQYLLCLGMPPALCIDYPWRWSKAIPMNSALIKWL YLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGINTDHLEPLRGEPNPI PNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVAGATRISIFGLGYLLACFYLLLFGTTLLQ KDTRAQLVLWDCLILYNVTVIISKNMLSLLSCVFVEQMQSNFCWVIQLFSLVCTVKGYYD PKEMMTRDRDCLLPVEEAGIIWDSICFFFLLLQRRIFLSHYFLHVSADLKATALQASRGF ALYNAANLKSINFHRQIEEKSLAQLKRQMKRIRAKQEKYRQSQASRGQLQSKDPQDPSQE PGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEALPEDPRPAAQSAFQM AYQAWVTNAQTVLRQRRERARQERAEQLASGGDLNPDVEPVDVPEDEMAGRSHMMQRVLS TMQFLWVLGQATVDGLTRWLRAFTKHHRTMSDVLCAERYLLTQELLRVGEVRRGVLDQLY VGEDEATLSGPVETRDGPSTASSGLGAEEPLSSMTDDTSSPLSTGYNTRSGSEEIVTDAG DLQAGTSLHGSQELLANARTRMRTASELLLDRRLHIPELEEAERFEAQQGRTLRLLRAGY QCVAAHSELLCYFIIILNHMVTASAASLVLPVLVFLWAMLTIPRPSKRFWMTAIVFTEVM VVTKYLFQFGFFPWNSYVVLRRYENKPYFPPRILGLEKTDSYIKYDLVQLMALFFHRSQL LCYGLWDHEEDRYPKDHCRSSVKDREAKEEPEAKLESQSETGTGHPKEPVLAGTPRDHIQ GKGSIRSKDVIQDPPEDLKPRHTRHISIRFRRRKETPGPKGTAVMETEHEEGEGKETTER KRPRHTQEKSKFRERMKAAGRRLQSFCVSLAQSFYQPLQRFFHDILHTKYRAATDVYALM FLADIVDIIIIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLR KTVLGKLAFQVVLVVAIHIWMFFILPAVTERMFSQNAVAQLWYFVKCIYFALSAYQIRCG YPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYA NIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVV NQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFISQYSPED IVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTVEYTNEKH TLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLG VRIQLRREQVGTGASGEQAGSRLEEELRRRLTETKASDFLEWWVIELQDCKADCNLLPMV IFSDKVSPPSLGFLAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLC QDIFLVRETRELELEEELYAKLIFLYRSPETMIKWTRERES
Lipid composition and mechanical force underlie multi-modal regulation of Piezo1 gating. Vaisey, G., MacKinnon, R. Sci Adv (2026) 12:eaed7115-eaed7115. DOI 10.1126/sciadv.aed7115 · PubMed
Other PDB entries of the same protein (UniProt E2JF22 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 11YE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.