Transition state structure of Cpf1(Cas12a) I1 conformation. Determined by electron microscopy at 3.91 Å resolution. Released 19 Dec 2018.
Explore 6GTC in 3D Show helices and sheets RCSB PDB PDBe
6GTC contains 58 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 |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| β-strand | 8 | 1 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 16-23 | 8 | 3 |
| α-helix | 27-34 | 8 | |
| α-helix | 38-43 | 6 | |
| α-helix | 46-48 | 3 | |
| α-helix | 51-63 | 13 | |
| α-helix | 74-88 | 15 | |
| α-helix | 95-106 | 12 | |
| α-helix | 110-113 | 4 | |
| α-helix | 125-127 | 3 | |
| α-helix | 137-147 | 11 | |
| α-helix | 162-169 | 8 | |
| α-helix | 208-211 | 4 | |
| α-helix | 213-222 | 10 | |
| α-helix | 231-237 | 7 | |
| β-strand | 243-244 | 2 | 4 |
| β-strand | 256-257 | 2 | 4 |
| α-helix | 258-259 | 2 | |
| α-helix | 278-284 | 7 | |
| β-strand | 288-290 | 3 | 5 |
| β-strand | 295-297 | 3 | 5 |
| α-helix | 300-310 | 11 | |
| α-helix | 324-327 | 4 | |
| α-helix | 370-380 | 11 | |
| β-strand | 392-394 | 3 | 6 |
| α-helix | 399-407 | 9 | |
| α-helix | 413-425 | 13 | |
| β-strand | 450-452 | 3 | 6 |
| α-helix | 453-463 | 11 | |
| α-helix | 464-466 | 3 | |
| α-helix | 476-482 | 7 | |
| α-helix | 488-498 | 11 | |
| α-helix | 520-522 | 3 | |
| α-helix | 524-527 | 4 | |
| α-helix | 561-564 | 4 | |
| α-helix | 576-579 | 4 | |
| β-strand | 595-597 | 3 | 3 |
| β-strand | 619-623 | 5 | 3 |
| β-strand | 628-633 | 6 | 3 |
| β-strand | 657-661 | 5 | 7 |
| α-helix | 669-673 | 5 | |
| α-helix | 680-682 | 3 | |
| α-helix | 686-694 | 9 | |
| α-helix | 716-718 | 3 | |
| α-helix | 720-728 | 9 | |
| α-helix | 744-746 | 3 | |
| α-helix | 751-757 | 7 | |
| β-strand | 762-766 | 5 | 7 |
| α-helix | 771-774 | 4 | |
| α-helix | 777-780 | 4 | |
| β-strand | 783-789 | 7 | 3 |
| α-helix | 803-806 | 4 | |
| α-helix | 808-810 | 3 | |
| α-helix | 814-818 | 5 | |
| β-strand | 823-824 | 2 | 8 |
| β-strand | 829-833 | 5 | 3 |
| β-strand | 841-843 | 3 | 9 |
| β-strand | 848 | 1 | 10 |
| β-strand | 862 | 1 | 10 |
| β-strand | 867-868 | 2 | 9 |
| α-helix | 871-873 | 3 | |
| β-strand | 877-883 | 7 | 3 |
| β-strand | 884-885 | 2 | 8 |
| β-strand | 886 | 1 | 2 |
| α-helix | 896-901 | 6 | |
| α-helix | 904-906 | 3 | |
| α-helix | 908-910 | 3 | |
| β-strand | 927-929 | 3 | 11 |
| β-strand | 935-938 | 4 | 11 |
| β-strand | 943-944 | 2 | 12 |
| β-strand | 951-952 | 2 | 12 |
| α-helix | 953-958 | 6 | |
| α-helix | 971-993 | 23 | |
| α-helix | 995-998 | 4 | |
| β-strand | 1003-1006 | 4 | 13 |
| α-helix | 1022-1025 | 4 | |
| β-strand | 1038 | 1 | 1 |
| β-strand | 1055 | 1 | 1 |
| α-helix | 1065-1067 | 3 | |
| β-strand | 1070 | 1 | 13 |
| β-strand | 1074-1077 | 4 | 13 |
| α-helix | 1104-1111 | 8 | |
| β-strand | 1114-1117 | 4 | 14 |
| β-strand | 1124-1127 | 4 | 14 |
| α-helix | 1130-1132 | 3 | |
| β-strand | 1144 | 1 | 14 |
| β-strand | 1150-1153 | 4 | 15 |
| β-strand | 1165-1168 | 4 | 15 |
| α-helix | 1170-1179 | 10 | |
| α-helix | 1192-1197 | 6 | |
| α-helix | 1201-1211 | 11 | |
| β-strand | 1219-1220 | 2 | 16 |
| β-strand | 1227-1228 | 2 | 16 |
| β-strand | 1230 | 1 | 17 |
| β-strand | 1242 | 1 | 17 |
| α-helix | 1243-1245 | 3 | |
| α-helix | 1257-1274 | 18 | |
| α-helix | 1288-1294 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CRISPR-associated endonuclease Cas12a | A | protein | 1329 | Francisella tularensis subsp. novicida 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*g)-3') | D | DNA | 55 | Francisella tularensis subsp. novicida U112 |
>6GTC_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
>6GTC_2 RNA (28-MER) (chains B) AAUUUCUACUGUUGUAGAUGAGAAGUCAUUUAAUAAGGCCACU
>6GTC_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
>6GTC_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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