Activated Leptotrichia buccalis (Lbu) CRISPR-Cas13a bound to AI-designed anti-CRISPR AIcrVIA1. Determined by electron microscopy at 3.43 Å resolution. Released 25 Feb 2026.
Explore 9MVS in 3D Show helices and sheets RCSB PDB PDBe
9MVS contains 65 α-helices and 18 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 9-13 | 5 | 2 |
| β-strand | 18-22 | 5 | 2 |
| α-helix | 30-37 | 8 | |
| β-strand | 39-41 | 3 | 3 |
| α-helix | 42-44 | 3 | |
| α-helix | 55-68 | 14 | |
| β-strand | 72-76 | 5 | 3 |
| β-strand | 79-83 | 5 | 3 |
| α-helix | 107-118 | 12 | |
| α-helix | 124-149 | 26 | |
| β-strand | 155-158 | 4 | 4 |
| β-strand | 165-168 | 4 | 4 |
| α-helix | 171-178 | 8 | |
| α-helix | 185-199 | 15 | |
| α-helix | 202-213 | 12 | |
| α-helix | 220-231 | 12 | |
| α-helix | 233-235 | 3 | |
| α-helix | 236-240 | 5 | |
| α-helix | 241-250 | 10 | |
| α-helix | 254-260 | 7 | |
| α-helix | 266-272 | 7 | |
| α-helix | 273-277 | 5 | |
| α-helix | 285-288 | 4 | |
| α-helix | 291-303 | 13 | |
| α-helix | 304-309 | 6 | |
| α-helix | 319-322 | 4 | |
| α-helix | 326-354 | 29 | |
| β-strand | 360 | 1 | 4 |
| α-helix | 363-376 | 14 | |
| α-helix | 380-393 | 14 | |
| β-strand | 409-411 | 3 | 5 |
| β-strand | 419-421 | 3 | 5 |
| α-helix | 424-431 | 8 | |
| α-helix | 434-444 | 11 | |
| α-helix | 454-475 | 22 | |
| α-helix | 484-486 | 3 | |
| α-helix | 497-506 | 10 | |
| α-helix | 509-522 | 14 | |
| α-helix | 531-540 | 10 | |
| α-helix | 554-555 | 2 | |
| α-helix | 556-569 | 14 | |
| α-helix | 582-599 | 18 | |
| α-helix | 600-604 | 5 | |
| α-helix | 605-608 | 4 | |
| α-helix | 615-628 | 14 | |
| α-helix | 651-665 | 15 | |
| α-helix | 676-696 | 21 | |
| α-helix | 699-703 | 5 | |
| α-helix | 708-713 | 6 | |
| α-helix | 717-731 | 15 | |
| α-helix | 734-737 | 4 | |
| α-helix | 738-746 | 9 | |
| α-helix | 753-755 | 3 | |
| α-helix | 757-768 | 12 | |
| α-helix | 771-787 | 17 | |
| α-helix | 794-804 | 11 | |
| α-helix | 818-822 | 5 | |
| α-helix | 835-841 | 7 | |
| β-strand | 848 | 1 | 6 |
| β-strand | 853 | 1 | 6 |
| α-helix | 857-865 | 9 | |
| α-helix | 868-878 | 11 | |
| α-helix | 884-912 | 29 | |
| α-helix | 922-946 | 25 | |
| α-helix | 948-982 | 35 | |
| α-helix | 988-993 | 6 | |
| α-helix | 1008-1019 | 12 | |
| α-helix | 1024-1029 | 6 | |
| α-helix | 1032-1041 | 10 | |
| α-helix | 1046-1052 | 7 | |
| α-helix | 1064-1074 | 11 | |
| α-helix | 1079-1082 | 4 | |
| α-helix | 1085-1095 | 11 | |
| β-strand | 1098-1103 | 6 | 7 |
| β-strand | 1111-1117 | 7 | 7 |
| α-helix | 1118 | 1 | |
| β-strand | 1119-1122 | 4 | 8 |
| β-strand | 1131-1134 | 4 | 8 |
| α-helix | 1138-1149 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-10 | 8 | 1 |
| α-helix | 15-32 | 18 | |
| β-strand | 35-42 | 8 | 1 |
| α-helix | 49-75 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AIcrVIA1 | B | protein | 83 | synthetic construct | |
| CRISPR-associated endoribonuclease Cas13a | A | protein | 1162 | Leptotrichia buccalis | C7NBY4 (AlphaFold model) |
| crRNA | C | RNA | 56 | Leptotrichia buccalis | |
| Guide complementary activator RNA (aRNA) | D | RNA | 26 | synthetic construct |
>9MVS_1 AIcrVIA1 (chains B) MKTIKVDVIVVGDDEELVEEYKKEAELIGKEYGVKIEVEPYFLEEGKFPWLDVDFAYNTT QEELDKAEKEAKKIAGSHHHHHH
>9MVS_2 CRISPR-associated endoribonuclease Cas13a (chains A) SNAMKVTKVGGISHKKYTSEGRLVKSESEENRTDERLSALLNMRLDMYIKNPSSTETKEN QKRIGKLKKFFSNKMVYLKDNTLSLKNGKKENIDREYSETDILESDVRDKKNFAVLKKIY LNENVNSEELEVFRNDIKKKLNKINSLKYSFEKNKANYQKINENNIEKVEGKSKRNIIYD YYRESAKRDAYVSNVKEAFDKLYKEEDIAKLVLEIENLTKLEKYKIREFYHEIIGRKNDK ENFAKIIYEEIQNVNNMKELIEKVPDMSELKKSQVFYKYYLDKEELNDKNIKYAFCHFVE IEMSQLLKNYVYKRLSNISNDKIKRIFEYQNLKKLIENKLLNKLDTYVRNCGKYNYYLQD GEIATSDFIARNRQNEAFLRNIIGVSSVAYFSLRNILETENENDITGRMRGKTVKNNKGE EKYVSGEVDKIYNENKKNEVKENLKMFYSYDFNMDNKNEIEDFFANIDEAISSIRHGIVH FNLELEGKDIFAFKNIAPSEISKKMFQNEINEKKLKLKIFRQLNSANVFRYLEKYKILNY LKRTRFEFVNKNIPFVPSFTKLYSRIDDLKNSLGIYWKTPKTNDDNKTKEIIDAQIYLLK NIYYGEFLNYFMSNNGNFFEISKEIIELNKNDKRNLKTGFYKLQKFEDIQEKIPKEYLAN IQSLYMINAGNQDEEEKDTYIDFIQKIFLKGFMTYLANNGRLSLIYIGSDEETNTSLAEK KQEFDKFLKKYEQNNNIKIPYEINEFLREIKLGNILKYTERLNMFYLILKLLNHKELTNL KGSLEKYQSANKEEAFSDQLELINLLNLDNNRVTEDFELEADEIGKFLDFNGNKVKDNKE LKKFDTNKIYFDGENIIKHRAFYNIKKYGMLNLLEKIADKAGYKISIEELKKYSNKKNEI EKNHKMQENLHRKYARPRKDEKFTDEDYESYKQAIENIEEYTHLKNKVEFNELNLLQGLL LRILHRLVGYTSIWERDLRFRLKGEFPENQYIEEIFNFENKKNVKYKGGQIVEKYIKFYK ELHQNDEVKINKYSSANIKVLKQEKKDLYIRNYIAHFNYIPHAEISLLEVLENLRKLLSY DRKLKNAVMKSVVDILKEYGFVATFKIGADKKIGIQTLESEKIVHLKNLKKKKLMTDRNS EELCKLVKIMFEYKMEEKKSEN
>9MVS_3 crRNA (chains C) UAGACCACCCCAAAAAUGAAGGGGACUAAAACUUUCUUUCUUUCCUUUUUCUGCCG
>9MVS_4 Guide complementary activator RNA (aRNA) (chains D) CGGCAGAAAAAGGAAAGAAAGAAACC
De novo design of potent CRISPR-Cas13 inhibitors. Taveneau, C., Chai, H.X., D'Silva, J. et al. Nat Chem Biol (2026) 22:1342-1350. DOI 10.1038/s41589-025-02136-3 · PubMed
Other PDB entries of the same protein (UniProt C7NBY4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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