Transient state structure of CRISPR-Cpf1 (Cas12a) I2 conformation. Determined by electron microscopy at 4.24 Å resolution. Released 19 Dec 2018.
Explore 6GTD in 3D Show helices and sheets RCSB PDB PDBe
6GTD contains 70 α-helices and 42 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 | 22 | 1 | 2 |
| α-helix | 27-34 | 8 | |
| α-helix | 37-39 | 3 | |
| α-helix | 50-53 | 4 | |
| α-helix | 60-63 | 4 | |
| α-helix | 73-87 | 15 | |
| α-helix | 96-108 | 13 | |
| α-helix | 110-113 | 4 | |
| α-helix | 118-120 | 3 | |
| α-helix | 137-148 | 12 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-170 | 6 | |
| α-helix | 199-201 | 3 | |
| α-helix | 208-214 | 7 | |
| α-helix | 219-223 | 5 | |
| α-helix | 231-234 | 4 | |
| α-helix | 240-242 | 3 | |
| β-strand | 243-244 | 2 | 3 |
| β-strand | 256-257 | 2 | 3 |
| α-helix | 258-259 | 2 | |
| α-helix | 282-285 | 4 | |
| β-strand | 287-288 | 2 | 4 |
| β-strand | 297-298 | 2 | 4 |
| α-helix | 301-305 | 5 | |
| α-helix | 306-311 | 6 | |
| α-helix | 357-361 | 5 | |
| β-strand | 363-364 | 2 | 5 |
| β-strand | 368-369 | 2 | 5 |
| α-helix | 370-372 | 3 | |
| α-helix | 373-377 | 5 | |
| α-helix | 381-383 | 3 | |
| β-strand | 392-394 | 3 | 6 |
| α-helix | 397-400 | 4 | |
| α-helix | 402-407 | 6 | |
| α-helix | 410-413 | 4 | |
| α-helix | 414-417 | 4 | |
| α-helix | 422-425 | 4 | |
| α-helix | 439-442 | 4 | |
| β-strand | 450-452 | 3 | 6 |
| α-helix | 453 | 1 | |
| α-helix | 454-458 | 5 | |
| α-helix | 459-461 | 3 | |
| α-helix | 462-465 | 4 | |
| α-helix | 469-471 | 3 | |
| α-helix | 477-483 | 7 | |
| α-helix | 485-487 | 3 | |
| α-helix | 488-494 | 7 | |
| α-helix | 495-497 | 3 | |
| α-helix | 517-519 | 3 | |
| α-helix | 520-525 | 6 | |
| α-helix | 531-533 | 3 | |
| α-helix | 534-539 | 6 | |
| α-helix | 559-561 | 3 | |
| α-helix | 566-569 | 4 | |
| α-helix | 576-578 | 3 | |
| β-strand | 597-598 | 2 | 7 |
| β-strand | 608 | 1 | 8 |
| β-strand | 618 | 1 | 8 |
| β-strand | 623 | 1 | 9 |
| β-strand | 628 | 1 | 9 |
| α-helix | 632 | 1 | |
| β-strand | 633 | 1 | 10 |
| α-helix | 634 | 1 | |
| α-helix | 643-648 | 6 | |
| β-strand | 652 | 1 | 11 |
| β-strand | 657-661 | 5 | 12 |
| α-helix | 669-671 | 3 | |
| α-helix | 676-678 | 3 | |
| α-helix | 686-689 | 4 | |
| α-helix | 714-729 | 16 | |
| α-helix | 734-737 | 4 | |
| α-helix | 750-753 | 4 | |
| β-strand | 762-766 | 5 | 12 |
| β-strand | 769 | 1 | 11 |
| α-helix | 773-780 | 8 | |
| β-strand | 783 | 1 | 10 |
| β-strand | 787 | 1 | 2 |
| β-strand | 822 | 1 | 13 |
| β-strand | 830-831 | 2 | 7 |
| β-strand | 843 | 1 | 14 |
| β-strand | 867 | 1 | 14 |
| α-helix | 872-874 | 3 | |
| β-strand | 886 | 1 | 13 |
| α-helix | 896-903 | 8 | |
| β-strand | 912 | 1 | 15 |
| β-strand | 913 | 1 | 16 |
| β-strand | 916-917 | 2 | 16 |
| β-strand | 925-929 | 5 | 16 |
| β-strand | 935-940 | 6 | 16 |
| β-strand | 943 | 1 | 17 |
| β-strand | 952 | 1 | 17 |
| α-helix | 956-960 | 5 | |
| α-helix | 971-984 | 14 | |
| α-helix | 986-996 | 11 | |
| β-strand | 1001 | 1 | 15 |
| β-strand | 1037 | 1 | 18 |
| α-helix | 1054 | 1 | |
| β-strand | 1055 | 1 | 1 |
| β-strand | 1056 | 1 | 18 |
| α-helix | 1064-1066 | 3 | |
| β-strand | 1071 | 1 | 19 |
| β-strand | 1074 | 1 | 19 |
| α-helix | 1102-1111 | 10 | |
| β-strand | 1150-1152 | 3 | 20 |
| β-strand | 1166-1168 | 3 | 20 |
| α-helix | 1175-1178 | 4 | |
| α-helix | 1192-1197 | 6 | |
| α-helix | 1201-1212 | 12 | |
| α-helix | 1262-1266 | 5 | |
| α-helix | 1270-1274 | 5 | |
| α-helix | 1288-1296 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CRISPR-associated endonuclease Cas12a | A | protein | 1329 | Francisella tularensis subsp. novicida (strain U112) | A0Q7Q2 (AlphaFold model) |
| RNA (28-mer) | B | RNA | 43 | Francisella tularensis subsp. novicida U112 | |
| DNA (5'-d(p*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*gp*t)-3') | D | DNA | 55 | Francisella tularensis subsp. novicida U112 |
>6GTD_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
>6GTD_2 RNA (28-MER) (chains B) AAUUUCUACUGUUGUAGAUGAGAAGUCAUUUAAUAAGGCCACU
>6GTD_3 DNA (5'-D(P*TP*GP*AP*CP*TP*TP*CP*TP*CP*TP*AP*AP*CP*AP*AP*GP*CP*TP*CP*G)-3') (chains C) ATTGCTTGCTCGATGCATGCAGTGGCCTTATTAAATGACTTCTCTAACGAGCTCG
>6GTD_4 DNA (5'-D(P*CP*GP*AP*GP*CP*TP*CP*GP*TP*TP*AP*GP*AP*GP*AP*AP*GP*T)-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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