Transient state structure of CRISPR-Cpf1 (Cas12a) I3 conformation. Determined by electron microscopy at 4.07 Å resolution. Released 19 Dec 2018.
Explore 6GTE in 3D Show helices and sheets RCSB PDB PDBe
6GTE contains 71 α-helices and 41 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 |
|---|---|---|---|
| β-strand | 8 | 1 | 1 |
| β-strand | 17-23 | 7 | 2 |
| α-helix | 27-31 | 5 | |
| α-helix | 50-52 | 3 | |
| α-helix | 58-62 | 5 | |
| α-helix | 76-84 | 9 | |
| α-helix | 98-113 | 16 | |
| α-helix | 120-122 | 3 | |
| α-helix | 137-142 | 6 | |
| α-helix | 162-170 | 9 | |
| α-helix | 200-206 | 7 | |
| α-helix | 212-219 | 8 | |
| α-helix | 230-233 | 4 | |
| α-helix | 256-258 | 3 | |
| α-helix | 266-268 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 296-298 | 3 | |
| α-helix | 300-302 | 3 | |
| α-helix | 304-307 | 4 | |
| α-helix | 314-319 | 6 | |
| α-helix | 324-327 | 4 | |
| α-helix | 347-356 | 10 | |
| α-helix | 358-361 | 4 | |
| β-strand | 363 | 1 | 3 |
| β-strand | 369 | 1 | 3 |
| α-helix | 370-377 | 8 | |
| α-helix | 400-402 | 3 | |
| α-helix | 403-407 | 5 | |
| α-helix | 413-415 | 3 | |
| α-helix | 418-421 | 4 | |
| α-helix | 454-459 | 6 | |
| α-helix | 461-464 | 4 | |
| α-helix | 485-494 | 10 | |
| α-helix | 497-499 | 3 | |
| α-helix | 500-505 | 6 | |
| α-helix | 517-519 | 3 | |
| α-helix | 523-527 | 5 | |
| α-helix | 529-531 | 3 | |
| α-helix | 534-539 | 6 | |
| α-helix | 540-543 | 4 | |
| α-helix | 565-568 | 4 | |
| α-helix | 569-574 | 6 | |
| α-helix | 575-579 | 5 | |
| α-helix | 583-587 | 5 | |
| β-strand | 596-598 | 3 | 2 |
| α-helix | 611-613 | 3 | |
| α-helix | 614-617 | 4 | |
| β-strand | 620-623 | 4 | 2 |
| β-strand | 628-631 | 4 | 2 |
| α-helix | 644-647 | 4 | |
| β-strand | 653-654 | 2 | 4 |
| β-strand | 655-656 | 2 | 2 |
| β-strand | 657-661 | 5 | 5 |
| α-helix | 665-672 | 8 | |
| α-helix | 679-682 | 4 | |
| α-helix | 686-694 | 9 | |
| α-helix | 715-724 | 10 | |
| α-helix | 734-737 | 4 | |
| α-helix | 741-743 | 3 | |
| α-helix | 744-746 | 3 | |
| α-helix | 751-754 | 4 | |
| β-strand | 762-766 | 5 | 5 |
| β-strand | 769-770 | 2 | 4 |
| α-helix | 771-780 | 10 | |
| β-strand | 785-789 | 5 | 2 |
| α-helix | 808-811 | 4 | |
| β-strand | 822-824 | 3 | 6 |
| β-strand | 829-833 | 5 | 2 |
| α-helix | 834-835 | 2 | |
| β-strand | 877-882 | 6 | 2 |
| β-strand | 884-886 | 3 | 6 |
| α-helix | 896-904 | 9 | |
| β-strand | 912-913 | 2 | 7 |
| β-strand | 925-929 | 5 | 7 |
| β-strand | 935-940 | 6 | 7 |
| β-strand | 943 | 1 | 8 |
| β-strand | 952 | 1 | 8 |
| α-helix | 954-960 | 7 | |
| α-helix | 980-998 | 19 | |
| β-strand | 1001-1002 | 2 | 7 |
| β-strand | 1003 | 1 | 9 |
| β-strand | 1006 | 1 | 10 |
| α-helix | 1026-1032 | 7 | |
| β-strand | 1038 | 1 | 1 |
| α-helix | 1044 | 1 | |
| β-strand | 1055 | 1 | 1 |
| β-strand | 1070 | 1 | 11 |
| β-strand | 1074 | 1 | 9 |
| β-strand | 1075 | 1 | 11 |
| β-strand | 1077 | 1 | 10 |
| α-helix | 1103-1110 | 8 | |
| β-strand | 1114 | 1 | 12 |
| β-strand | 1117 | 1 | 13 |
| β-strand | 1124 | 1 | 13 |
| β-strand | 1125-1126 | 2 | 14 |
| β-strand | 1127 | 1 | 12 |
| α-helix | 1130-1132 | 3 | |
| β-strand | 1144-1145 | 2 | 14 |
| β-strand | 1150 | 1 | 15 |
| β-strand | 1168 | 1 | 15 |
| α-helix | 1170-1177 | 8 | |
| α-helix | 1192-1197 | 6 | |
| α-helix | 1201-1212 | 12 | |
| β-strand | 1218 | 1 | 16 |
| β-strand | 1229 | 1 | 16 |
| α-helix | 1243-1245 | 3 | |
| α-helix | 1257-1260 | 4 | |
| α-helix | 1262-1265 | 4 | |
| α-helix | 1266-1268 | 3 | |
| α-helix | 1269-1273 | 5 | |
| α-helix | 1288-1294 | 7 | |
| α-helix | 1295-1297 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CRISPR-associated endonuclease Cas12a | A | protein | 1329 | Francisella tularensis subsp. novicida (strain U112) | A0Q7Q2 (AlphaFold model) |
| RNA (29-mer) | B | RNA | 43 | Francisella tularensis subsp. novicida U112 | |
| DNA (5'-d(p*ap*tp*gp*ap*cp*tp*tp*cp*tp*cp*tp*ap*ap*cp*ap*ap*gp*cp*tp*cp*g)-3') | C | DNA | 55 | Francisella tularensis subsp. novicida U112 | |
| DNA (5'-d(p*cp*gp*ap*gp*cp*tp*cp*gp*tp*tp*ap*gp*ap*gp*ap*ap*g)-3') | D | DNA | 55 | Francisella tularensis subsp. novicida U112 |
>6GTE_1 CRISPR-associated endonuclease Cas12a (chains A) MSIYQEFVNKYSLSKTLRFELIPQGKTLENIKARGLILDDEKRAKDYKKAKQIIDKYHQF FIEEILSSVCISEDLLQNYSDVYFKLKKSDDDNLQKDFKSAKDTIKKQISEYIKDSEKFK NLFNQNLIDAKKGQESDLILWLKQSKDNGIELFKANSDITDIDEALEIIKSFKGWTTYFK GFHENRKNVYSSNDIPTSIIYRIVDDNLPKFLENKAKYESLKDKAPEAINYEQIKKDLAE ELTFDIDYKTSEVNQRVFSLDEVFEIANFNNYLNQSGITKFNTIIGGKFVNGENTKRKGI NEYINLYSQQINDKTLKKYKMSVLFKQILSDTESKSFVIDKLEDDSDVVTTMQSFYEQIA AFKTVEEKSIKETLSLLFDDLKAQKLDLSKIYFKNDKSLTDLSQQVFDDYSVIGTAVLEY ITQQIAPKNLDNPSKKEQELIAKKTEKAKYLSLETIKLALEEFNKHRDIDKQCRFEEILA NFAAIPMIFDEIAQNKDNLAQISIKYQNQGKKDLLQASAEDDVKAIKDLLDQTNNLLHKL KIFHISQSEDKANILDKDEHFYLVFEECYFELANIVPLYNKIRNYITQKPYSDEKFKLNF ENSTLANGWDKNKEPDNTAILFIKDDKYYLGVMNKKNNKIFDDKAIKENKGEGYKKIVYK LLPGANKMLPKVFFSAKSIKFYNPSEDILRIRNHSTHTKNGSPQKGYEKFEFNIEDCRKF IDFYKQSISKHPEWKDFGFRFSDTQRYNSIDEFYREVENQGYKLTFENISESYIDSVVNQ GKLYLFQIYNKDFSAYSKGRPNLHTLYWKALFDERNLQDVVYKLNGEAELFYRKQSIPKK ITHPAKEAIANKNKDNPKKESVFEYDLIKDKRFTEDKFFFHCPITINFKSSGANKFNDEI NLLLKEKANDVHILSIDRGERHLAYYTLVDGKGNIIKQDTFNIIGNDRMKTNYHDKLAAI EKDRDSARKDWKKINNIKEMKEGYLSQVVHEIAKLVIEYNAIVVFQDLNFGFKRGRFKVE KQVYQKLEKMLIEKLNYLVFKDNEFDKTGGVLRAYQLTAPFETFKKMGKQTGIIYYVPAG FTSKICPVTGFVNQLYPKYESVSKSQEFFSKFDKICYNLDKGYFEFSFDYKNFGDKAAKG KWTIASFGSRLINFRNSDKNHNWDTREVYPTKELEKLLKDYSIEYGHGECIKAAICGESD KKFFAKLTSVLNTILQMRNSKTGTELDYLISPVADVNGNFFDSRQAPKNMPQDADANGAY HIGLKGLMLLGRIKNNQEGKKLNLVIKNEEYFEFVQNRNNGSEFELENLYFQGELRRQAS ALEHHHHHH
>6GTE_2 RNA (29-MER) (chains B) AAUUUCUACUGUUGUAGAUGAGAAGUCAUUUAAUAAGGCCACU
>6GTE_3 DNA (5'-D(P*AP*TP*GP*AP*CP*TP*TP*CP*TP*CP*TP*AP*AP*CP*AP*AP*GP*CP*TP*CP*G)-3') (chains C) ATTGCTTGCTCGATGCATGCAGTGGCCTTATTAAATGACTTCTCTAACGAGCTCG
>6GTE_4 DNA (5'-D(P*CP*GP*AP*GP*CP*TP*CP*GP*TP*TP*AP*GP*AP*GP*AP*AP*G)-3') (chains D) CGAGCTCGTTAGAGAAGTCATTTAATAAGGCCACTGCATGCATCGAGCAAGCAAT
Conformational Activation Promotes CRISPR-Cas12a Catalysis and Resetting of the Endonuclease Activity. Stella, S., Mesa, P., Thomsen, J. et al. Cell (2018) 175:1856-1871.e21. DOI 10.1016/j.cell.2018.10.045 · PubMed
Other PDB entries of the same protein (UniProt A0Q7Q2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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