Cryo-EM structure of autoinhibited human talin-1. Determined by electron microscopy at 6.2 Å resolution. Released 16 Oct 2019.
Explore 6R9T in 3D Show helices and sheets RCSB PDB PDBe
6R9T contains 76 α-helices and 7 β-strands across 1 chain. 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 | 211-225 | 15 | |
| α-helix | 232-247 | 16 | |
| α-helix | 276-286 | 11 | |
| α-helix | 291-304 | 14 | |
| β-strand | 311-318 | 8 | 1 |
| β-strand | 325-332 | 8 | 1 |
| β-strand | 336-341 | 6 | 1 |
| β-strand | 347-352 | 6 | 1 |
| β-strand | 358-361 | 4 | 1 |
| β-strand | 366-369 | 4 | 1 |
| α-helix | 371-373 | 3 | |
| β-strand | 378-381 | 4 | 1 |
| α-helix | 385-393 | 9 | |
| α-helix | 490-511 | 22 | |
| α-helix | 512-514 | 3 | |
| α-helix | 519-521 | 3 | |
| α-helix | 526-560 | 35 | |
| α-helix | 570-601 | 32 | |
| α-helix | 606-625 | 20 | |
| α-helix | 634-655 | 22 | |
| α-helix | 662-692 | 31 | |
| α-helix | 698-722 | 25 | |
| α-helix | 733-754 | 22 | |
| α-helix | 761-789 | 29 | |
| α-helix | 802-808 | 7 | |
| α-helix | 810-814 | 5 | |
| α-helix | 819-845 | 27 | |
| α-helix | 852-879 | 28 | |
| α-helix | 884-913 | 30 | |
| α-helix | 914-918 | 5 | |
| α-helix | 919-939 | 21 | |
| α-helix | 953-975 | 23 | |
| α-helix | 980-1006 | 27 | |
| α-helix | 1014-1042 | 29 | |
| α-helix | 1049-1073 | 25 | |
| α-helix | 1077-1079 | 3 | |
| α-helix | 1084-1111 | 28 | |
| α-helix | 1116-1141 | 26 | |
| α-helix | 1145-1174 | 30 | |
| α-helix | 1179-1201 | 23 | |
| α-helix | 1209-1224 | 16 | |
| α-helix | 1235-1258 | 24 | |
| α-helix | 1264-1287 | 24 | |
| α-helix | 1295-1322 | 28 | |
| α-helix | 1329-1353 | 25 | |
| α-helix | 1360-1376 | 17 | |
| α-helix | 1389-1416 | 28 | |
| α-helix | 1419-1449 | 31 | |
| α-helix | 1464-1482 | 19 | |
| α-helix | 1488-1513 | 26 | |
| α-helix | 1519-1546 | 28 | |
| α-helix | 1552-1576 | 25 | |
| α-helix | 1579-1582 | 4 | |
| α-helix | 1590-1622 | 33 | |
| α-helix | 1627-1652 | 26 | |
| α-helix | 1658-1684 | 27 | |
| α-helix | 1695-1722 | 28 | |
| α-helix | 1724-1750 | 27 | |
| α-helix | 1755-1782 | 28 | |
| α-helix | 1791-1820 | 30 | |
| α-helix | 1827-1839 | 13 | |
| α-helix | 1850-1876 | 27 | |
| α-helix | 1879-1882 | 4 | |
| α-helix | 1883-1899 | 17 | |
| α-helix | 1903-1906 | 4 | |
| α-helix | 1910-1939 | 30 | |
| α-helix | 1945-1970 | 26 | |
| α-helix | 1976-2001 | 26 | |
| α-helix | 2016-2035 | 20 | |
| α-helix | 2041-2069 | 29 | |
| α-helix | 2075-2099 | 25 | |
| α-helix | 2109-2135 | 27 | |
| α-helix | 2141-2161 | 21 | |
| α-helix | 2172-2195 | 24 | |
| α-helix | 2198-2221 | 24 | |
| α-helix | 2233-2259 | 27 | |
| α-helix | 2263-2288 | 26 | |
| α-helix | 2301-2325 | 25 | |
| α-helix | 2341-2369 | 29 | |
| α-helix | 2370-2374 | 5 | |
| α-helix | 2383-2416 | 34 | |
| α-helix | 2421-2443 | 23 | |
| α-helix | 2453-2474 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Talin-1 | A | protein | 2547 | Homo sapiens | Q9Y490 (AlphaFold model) |
>6R9T_1 Talin-1 (chains A) MVALSLKISIGNVVKTMQFEPSTMVYDACRIIRERIPEAPAGPPSDFGLFLSDDDPKKGI WLEAGKALDYYMLRNGDTMEYRKKQRPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIG ITNHDEYSLVRELMEEKKEEITGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTL REQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAG FQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVK LARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWNLTNIKRWA ASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKKKSKDHFGLEGDEESTML EDSVSPKKSTVLQQQYNRVGKVEHGSVALPAIMRSGASGPENFQVGSMPPAQQQITSGQM HRGHMPPLTSAQQALTGTINSSMQAVQAAQATLDDFDTLPPLGQDAASKAWRKNKMDESK HEIHSQVDAITAGTASVVNLTAGDPAETDYTAVGCAVTTISSNLTEMSRGVKLLAALLED EGGSGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGELLQQIGESDT DPHFQDALMQLAKAVASAAAALVLKAKSVAQRTEDSGLQTQVIAAATQCALSTSQLVACT KVVAPTISSPVCQEQLVEAGRLVAKAVEGCVSASQAATEDGQLLRGVGAAATAVTQALNE LLQHVKAHATGAGPAGRYDQATDTILTVTENIFSSMGDAGEMVRQARILAQATSDLVNAI KADAEGESDLENSRKLLSAAKILADATAKMVEAAKGAAAHPDSEEQQQRLREAAEGLRMA TNAAAQNAIKKKLVQRLEHAAKQAAASATQTIAAAQHAASTPKASAGPQPLLVQSCKAVA EQIPLLVQGVRGSQAQPDSPSAQLALIAASQSFLQPGGKMVAAAKASVPTIQDQASAMQL SQCAKNLGTALAELRTAAQKAQEACGPLEMDSALSVVQNLEKDLQEVKAAARDGKLKPLP GETMEKCTQDLGNSTKAVSSAIAQLLGEVAQGNENYAGIAARDVAGGLRSLAQAARGVAA LTSDPAVQAIVLDTASDVLDKASSLIEEAKKAAGHPGDPESQQRLAQVAKAVTQALNRCV SCLPGQRDVDNALRAVGDASKRLLSDSLPPSTGTFQEAQSRLNEAAAGLNQAATELVQAS RGTPQDLARASGRFGQDFSTFLEAGVEMAGQAPSQEDRAQVVSNLKGISMSSSKLLLAAK ALSTDPAAPNLKSQLAAAARAVTDSINQLITMCTQQAPGQKECDNALRELETVRELLENP VQPINDMSYFGCLDSVMENSKVLGEAMTGISQNAKNGNLPEFGDAISTASKALCGFTEAA AQAAYLVGVSDPNSQAGQQGLVEPTQFARANQAIQMACQSLGEPGCTQAQVLSAATIVAK HTSALCNSCRLASARTTNPTAKRQFVQSAKEVANSTANLVKTIKALDGAFTEENRAQCRA ATAPLLEAVDNLSAFASNPEFSSIPAQISPEGRAAMEPIVISAKTMLESAGGLIQTARAL AVNPRDPPSWSVLAGHSRTVSDSIKKLITSMRDKAPGQLECETAIAALNSCLRDLDQASL AAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLANAARAEASQLGHKVSQMAQYFEP LTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKQAAHTQEALEEAV QMMTEAVEDLTTTLNEAASAAGVVGGMVDSITQAINQLDEGPMGEPEGSFVDYQTTMVRT AKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASEAKPAAVAAENEEIGSHIKHRV QELGHGCAALVTKAGALQCSPSDAYTKKELIECARRVSEKVSHVLAALQAGNRGTQACIT AASAVSGIIADLDTTIMFATAGTLNREGTETFADHREGILKTAKVLVEDTKVLVQNAAGS QEKLAQAAQSSVATITRLADVVKLGAASLGAEDPETQVVLINAVKDVAKALGDLISATKA AAGKVGDDPAVWQLKNSAKVMVTNVTSLLKTVKAVEDEATKGTRALEATTEHIRQELAVF CSPEPPAKTSTPEDFIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRRAIADMLRACK EAAYHPEVAPDVRLRALHYGRECANGYLELLDHVLLTLQKPSPELKQQLTGHSKRVAGSV TELIQAAEAMKGTEWVDPEDPTVIAENELLGAAAAIEAAAKKLEQLKPRAKPKEADESLN FEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALDDGQWSQGLISAARMV AAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAG NAVKRASDNLVKAAQKAAAFEEQENETVVVKEKMVGGIAQIIAAQEEMLRKERELEEARK KLAQIRQQQYKFLPSELRDEHLVVLFQ
The Architecture of Talin1 Reveals an Autoinhibition Mechanism. Dedden, D., Schumacher, S., Kelley, C.F. et al. Cell (2019) 179:120-131.e13. DOI 10.1016/j.cell.2019.08.034 · PubMed
Other PDB entries of the same protein (UniProt Q9Y490 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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