6GTG: CRISPR-associated endonuclease Cas12a

Transition state structure of Cpf1(Cas12a) I4 conformation. Determined by electron microscopy at 3.27 Å resolution. Released 19 Dec 2018.

Method
Electron microscopy
Resolution
3.27 Å
Organism
Francisella tularensis subsp. novicida U112
Chains
4
Atoms
12,538
Mol. weight
203.38 kDa
Ligands
MG
Released
19 Dec 2018

Explore 6GTG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6GTG contains 69 α-helices and 40 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.

Chain A: 69 helices, 40 β-strands

ElementResiduesLengthSheet
β-strand811
β-strand15-1732
β-strand20-2343
α-helix27-348
α-helix49-513
α-helix54-574
α-helix75-8410
α-helix96-10914
α-helix117-1193
α-helix125-1284
β-strand13114
β-strand13414
α-helix137-1426
α-helix143-1475
α-helix165-1706
α-helix176-1794
α-helix199-2024
α-helix203-2075
α-helix209-2168
α-helix219-2224
α-helix237-2393
β-strand24615
β-strand25215
α-helix256-2583
α-helix266-2716
α-helix275-2773
α-helix282-2854
β-strand28816
β-strand29716
α-helix300-3034
α-helix305-3117
α-helix316-3183
α-helix321-3277
α-helix345-3484
α-helix351-3599
α-helix371-3733
β-strand39217
α-helix398-4069
α-helix414-4218
β-strand45217
α-helix454-46310
α-helix475-4817
α-helix485-4873
α-helix488-4914
α-helix495-4984
α-helix517-5193
α-helix523-53412
α-helix536-5383
α-helix565-5728
α-helix579-5868
α-helix589-5902
α-helix592-5943
β-strand595-59733
α-helix5981
α-helix611-6133
α-helix614-6174
β-strand620-62343
β-strand628-63363
α-helix643-6475
β-strand655-66178
α-helix665-6728
α-helix679-6824
α-helix688-6947
α-helix701-7044
α-helix719-7224
α-helix751-7588
β-strand762-76878
α-helix771-7788
β-strand783-78973
β-strand822-82432
β-strand829-83353
β-strand879-88133
β-strand882-88652
α-helix888-8903
α-helix896-90611
β-strand91219
β-strand913110
β-strand915-916211
β-strand925-927312
β-strand929110
β-strand938-940312
β-strand943-944213
β-strand951-952213
α-helix953-97018
α-helix978-99821
β-strand100119
β-strand1004-1006311
α-helix1010-10156
α-helix1016-10183
α-helix1026-10327
β-strand103811
α-helix10441
β-strand105511
β-strand1070-1071211
β-strand1074-1077411
α-helix1103-11086
β-strand1116-1117214
β-strand1124-1125214
α-helix1130-11323
β-strand1145114
α-helix1171-118010
α-helix1192-11976
α-helix1203-121412
β-strand1230115
β-strand1242115
α-helix1243-12453
α-helix1255-126511
α-helix1269-12746
α-helix1291-12966

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CRISPR-associated endonuclease Cas12aAprotein1329Francisella tularensis subsp. novicida U112A0Q7Q2 (AlphaFold model)
RNA (40-mer)BRNA43Francisella tularensis subsp. novicida U112
DNA (32-mer)CDNA55Francisella 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')DDNA55Francisella tularensis subsp. novicida U112
Sequence of entity 1 (A), FASTA
>6GTG_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
Sequence of entity 2 (B), FASTA
>6GTG_2 RNA (40-MER) (chains B)
AAUUUCUACUGUUGUAGAUGAGAAGUCAUUUAAUAAGGCCACU
Sequence of entity 3 (C), FASTA
>6GTG_3 DNA (32-MER) (chains C)
ATTGCTTGCTCGATGCATGCAGTGGCCTTATTAAATGACTTCTCTAACGAGCTCG
Sequence of entity 4 (D), FASTA
>6GTG_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

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg4

Primary citation

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:

Browse structure collections

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