The Flattened Structure of mPIEZO1 in Lipid Bilayer. Determined by electron microscopy at 6.81 Å resolution. Released 13 Apr 2022.
Explore 7WLU in 3D Show helices and sheets RCSB PDB PDBe
7WLU contains 204 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 577-584 | 8 | |
| α-helix | 587-597 | 11 | |
| α-helix | 605-624 | 20 | |
| α-helix | 626-630 | 5 | |
| α-helix | 632-652 | 21 | |
| α-helix | 657-666 | 10 | |
| α-helix | 671-676 | 6 | |
| α-helix | 683-705 | 23 | |
| α-helix | 708-715 | 8 | |
| α-helix | 785-823 | 39 | |
| α-helix | 829-839 | 11 | |
| α-helix | 845-866 | 22 | |
| α-helix | 925-949 | 25 | |
| α-helix | 966-972 | 7 | |
| α-helix | 974-1005 | 32 | |
| α-helix | 1008-1022 | 15 | |
| α-helix | 1026-1051 | 26 | |
| α-helix | 1074-1079 | 6 | |
| α-helix | 1092-1114 | 23 | |
| α-helix | 1117-1122 | 6 | |
| α-helix | 1140-1142 | 3 | |
| α-helix | 1149-1175 | 27 | |
| α-helix | 1179-1200 | 22 | |
| α-helix | 1203-1233 | 31 | |
| α-helix | 1236-1248 | 13 | |
| α-helix | 1281-1298 | 18 | |
| α-helix | 1302-1363 | 62 | |
| α-helix | 1405-1409 | 5 | |
| α-helix | 1439-1446 | 8 | |
| α-helix | 1449-1467 | 19 | |
| α-helix | 1491-1546 | 56 | |
| α-helix | 1552-1558 | 7 | |
| α-helix | 1657-1668 | 12 | |
| α-helix | 1673-1686 | 14 | |
| α-helix | 1689-1701 | 13 | |
| α-helix | 1705-1718 | 14 | |
| α-helix | 1729-1748 | 20 | |
| α-helix | 1771-1774 | 4 | |
| α-helix | 1786-1803 | 18 | |
| α-helix | 1942-1967 | 26 | |
| α-helix | 1977-1993 | 17 | |
| α-helix | 1996-1998 | 3 | |
| α-helix | 2007-2013 | 7 | |
| α-helix | 2018-2040 | 23 | |
| α-helix | 2043-2060 | 18 | |
| α-helix | 2065-2068 | 4 | |
| α-helix | 2078-2099 | 22 | |
| α-helix | 2111-2113 | 3 | |
| α-helix | 2116-2126 | 11 | |
| α-helix | 2131-2142 | 12 | |
| α-helix | 2149-2174 | 26 | |
| α-helix | 2176-2178 | 3 | |
| α-helix | 2185-2208 | 24 | |
| α-helix | 2209-2213 | 5 | |
| β-strand | 2219 | 1 | 1 |
| β-strand | 2223-2232 | 10 | 2 |
| β-strand | 2236-2243 | 8 | 2 |
| β-strand | 2248-2250 | 3 | 3 |
| α-helix | 2251-2252 | 2 | |
| α-helix | 2253-2262 | 10 | |
| α-helix | 2267-2275 | 9 | |
| α-helix | 2278-2280 | 3 | |
| β-strand | 2281-2284 | 4 | 3 |
| β-strand | 2286-2287 | 2 | 4 |
| α-helix | 2298-2309 | 12 | |
| β-strand | 2315-2325 | 11 | 2 |
| β-strand | 2335-2344 | 10 | 2 |
| α-helix | 2349-2357 | 9 | |
| β-strand | 2366-2372 | 7 | 5 |
| β-strand | 2375-2378 | 4 | 3 |
| α-helix | 2385 | 1 | |
| β-strand | 2386 | 1 | 3 |
| α-helix | 2387 | 1 | |
| β-strand | 2399-2409 | 11 | 5 |
| α-helix | 2423-2425 | 3 | |
| β-strand | 2426-2434 | 9 | 5 |
| β-strand | 2443-2444 | 2 | 4 |
| β-strand | 2447-2450 | 4 | 3 |
| β-strand | 2453 | 1 | 1 |
| α-helix | 2466-2485 | 20 | |
| α-helix | 2501-2516 | 16 | |
| α-helix | 2519-2534 | 16 | |
| α-helix | 2536-2541 | 6 | |
| α-helix | 2545-2546 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Piezo-type mechanosensitive ion channel component 1 | A, C, E | protein | 2547 | Mus musculus | E2JF22 (AlphaFold model) |
>7WLU_1 Piezo-type mechanosensitive ion channel component 1 (chains A, C, 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 VRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKVSPPSLGF LAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELE LEEELYAKLIFLYRSPETMIKWTRERE
| ID | Name | Formula | Copies |
|---|---|---|---|
| PLX | (9R,11S)-9-({[(1S)-1-hydroxyhexadecyl]oxy}methyl)-2,2-dimethyl-5,7,10-trioxa-2L… | C42 H89 N O8 P | 3 |
Structure deformation and curvature sensing of PIEZO1 in lipid membranes. Yang, X., Lin, C., Chen, X. et al. Nature (2022) 604:377-383. DOI 10.1038/s41586-022-04574-8 · PubMed
Other PDB entries of the same protein (UniProt E2JF22 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7WLU 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.