ACE2-B0AT1 complex, open conformation. Determined by electron microscopy at 4.5 Å resolution. Released 11 Mar 2020.
Explore 6M1D in 3D Show helices and sheets RCSB PDB PDBe
6M1D contains 155 α-helices and 41 β-strands across 4 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 | 21-24 | 4 | |
| α-helix | 39-49 | 11 | |
| α-helix | 58-62 | 5 | |
| α-helix | 71-77 | 7 | |
| α-helix | 78-82 | 5 | |
| α-helix | 83-96 | 14 | |
| α-helix | 100-106 | 7 | |
| α-helix | 114-141 | 28 | |
| β-strand | 155 | 1 | 1 |
| β-strand | 162 | 1 | 1 |
| α-helix | 164-168 | 5 | |
| α-helix | 171-174 | 4 | |
| α-helix | 175-180 | 6 | |
| α-helix | 195-211 | 17 | |
| α-helix | 215-221 | 7 | |
| α-helix | 229-243 | 15 | |
| α-helix | 259-261 | 3 | |
| α-helix | 265-278 | 14 | |
| α-helix | 285-289 | 5 | |
| α-helix | 300-347 | 48 | |
| α-helix | 360-370 | 11 | |
| α-helix | 374-376 | 3 | |
| α-helix | 397 | 1 | |
| α-helix | 398-402 | 5 | |
| α-helix | 403-407 | 5 | |
| α-helix | 413-430 | 18 | |
| α-helix | 434-440 | 7 | |
| α-helix | 455-463 | 9 | |
| α-helix | 469-474 | 6 | |
| α-helix | 478-487 | 10 | |
| α-helix | 493-503 | 11 | |
| α-helix | 504-510 | 7 | |
| α-helix | 511-521 | 11 | |
| α-helix | 528-532 | 5 | |
| α-helix | 533-537 | 5 | |
| α-helix | 538-551 | 14 | |
| β-strand | 560-562 | 3 | 2 |
| β-strand | 574-576 | 3 | 2 |
| α-helix | 586-607 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-31 | 10 | |
| α-helix | 37-48 | 12 | |
| α-helix | 60-76 | 17 | |
| α-helix | 110-112 | 3 | |
| α-helix | 116-128 | 13 | |
| β-strand | 131-133 | 3 | 3 |
| β-strand | 141-143 | 3 | 3 |
| α-helix | 144-147 | 4 | |
| α-helix | 149-153 | 5 | |
| α-helix | 158-169 | 12 | |
| α-helix | 173-176 | 4 | |
| α-helix | 177-179 | 3 | |
| α-helix | 181-193 | 13 | |
| α-helix | 199-203 | 5 | |
| α-helix | 204-207 | 4 | |
| α-helix | 230-251 | 22 | |
| β-strand | 260 | 1 | 4 |
| β-strand | 262-263 | 2 | 5 |
| α-helix | 276-278 | 3 | |
| α-helix | 306-316 | 11 | |
| β-strand | 334 | 1 | 6 |
| β-strand | 347-348 | 2 | 7 |
| β-strand | 358-359 | 2 | 7 |
| β-strand | 362 | 1 | 6 |
| α-helix | 367-382 | 16 | |
| α-helix | 399-406 | 8 | |
| α-helix | 409-412 | 4 | |
| α-helix | 424-426 | 3 | |
| α-helix | 435-442 | 8 | |
| α-helix | 443-447 | 5 | |
| α-helix | 450-464 | 15 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 5 |
| α-helix | 499-502 | 4 | |
| α-helix | 504-507 | 4 | |
| α-helix | 514-520 | 7 | |
| α-helix | 523-529 | 7 | |
| α-helix | 530-532 | 3 | |
| α-helix | 549-558 | 10 | |
| α-helix | 568-574 | 7 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-592 | 4 | |
| α-helix | 594-596 | 3 | |
| β-strand | 607 | 1 | 4 |
| α-helix | 614-616 | 3 | |
| β-strand | 618-621 | 4 | 8 |
| α-helix | 632-635 | 4 | |
| α-helix | 637-657 | 21 | |
| α-helix | 667-669 | 3 | |
| β-strand | 670-676 | 7 | 8 |
| β-strand | 680-685 | 6 | 8 |
| β-strand | 686 | 1 | 9 |
| β-strand | 694 | 1 | 9 |
| α-helix | 697-706 | 10 | |
| α-helix | 708-711 | 4 | |
| β-strand | 723 | 1 | 8 |
| α-helix | 742-766 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-31 | 10 | |
| α-helix | 37-48 | 12 | |
| α-helix | 58-60 | 3 | |
| α-helix | 64-76 | 13 | |
| α-helix | 91-94 | 4 | |
| α-helix | 110-112 | 3 | |
| α-helix | 116-128 | 13 | |
| β-strand | 131-133 | 3 | 12 |
| β-strand | 141-143 | 3 | 12 |
| α-helix | 144-147 | 4 | |
| α-helix | 149-153 | 5 | |
| α-helix | 158-169 | 12 | |
| α-helix | 173-176 | 4 | |
| α-helix | 177-179 | 3 | |
| α-helix | 181-193 | 13 | |
| α-helix | 199-203 | 5 | |
| α-helix | 204-207 | 4 | |
| β-strand | 210 | 1 | 13 |
| β-strand | 216 | 1 | 13 |
| α-helix | 230-251 | 22 | |
| β-strand | 260 | 1 | 14 |
| β-strand | 262-263 | 2 | 15 |
| α-helix | 276-278 | 3 | |
| α-helix | 306-316 | 11 | |
| β-strand | 347-348 | 2 | 16 |
| β-strand | 358-359 | 2 | 16 |
| α-helix | 367-382 | 16 | |
| α-helix | 398-406 | 9 | |
| α-helix | 409-412 | 4 | |
| α-helix | 424-426 | 3 | |
| α-helix | 435-442 | 8 | |
| α-helix | 443-447 | 5 | |
| α-helix | 450-464 | 15 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 15 |
| α-helix | 499-502 | 4 | |
| α-helix | 504-507 | 4 | |
| α-helix | 514-529 | 16 | |
| α-helix | 530-532 | 3 | |
| α-helix | 549-558 | 10 | |
| α-helix | 567-571 | 5 | |
| α-helix | 582-587 | 6 | |
| α-helix | 589-592 | 4 | |
| α-helix | 594-596 | 3 | |
| β-strand | 607 | 1 | 14 |
| α-helix | 614-616 | 3 | |
| β-strand | 618-620 | 3 | 17 |
| β-strand | 621 | 1 | 18 |
| α-helix | 632-635 | 4 | |
| α-helix | 637-657 | 21 | |
| α-helix | 667-669 | 3 | |
| β-strand | 670-676 | 7 | 17 |
| β-strand | 680-685 | 6 | 17 |
| β-strand | 686 | 1 | 19 |
| β-strand | 694 | 1 | 19 |
| α-helix | 697-706 | 10 | |
| α-helix | 708-711 | 4 | |
| β-strand | 723 | 1 | 18 |
| α-helix | 742-766 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium-dependent neutral amino acid transporter B(0)AT1 | A, C | protein | 654 | Homo sapiens | Q695T7 (AlphaFold model) |
| Angiotensin-converting enzyme 2 | B, D | protein | 814 | Homo sapiens | Q9BYF1 (AlphaFold model) |
>6M1D_1 Sodium-dependent neutral amino acid transporter B(0)AT1 (chains A, C) MADYKDDDDKSGPDEVDASGRVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQ YMLTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGS LGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQT GYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTG KAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFS LAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTN ILTLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAF IVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTG LICLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEF MIGHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPN WVYVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLKY
>6M1D_2 Angiotensin-converting enzyme 2 (chains B, D) MRSSSSWLLLSLVAVTAAWSHPQFEKQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYN TNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSED KSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSE VGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFE EIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNI DVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDL GKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLS AATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKD QWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQ AAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPL FTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAM RQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRI NDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKK NKARSGENPYASIDISKGENNPGFQNTDDVQTSF
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Yan, R., Zhang, Y., Li, Y. et al. Science (2020) 367:1444-1448. DOI 10.1126/science.abb2762 · PubMed
Other PDB entries of the same protein (UniProt Q695T7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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