5NFV: Catalytically inactive FnCas12 mutant

Crystal structure of catalytically inactive FnCas12 mutant bound to an R-loop structure containing a pre-crRNA mimic and full-length DNA target. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Jun 2017.

Method
X-ray diffraction
Resolution
2.5 Å
Organisms
Francisella tularensis subsp. novicida (strain U112), synthetic construct
Chains
4
Atoms
12,547
Mol. weight
190.5 kDa
Ligands
B3P, MG
Released
14 Jun 2017

Explore 5NFV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NFV contains 74 α-helices and 47 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: 74 helices, 47 β-strands

ElementResiduesLengthSheet
β-strand811
β-strand13-23112
α-helix27-348
α-helix36-6833
α-helix73-8614
α-helix92-11423
α-helix117-1204
α-helix125-1273
α-helix137-14711
α-helix153-1553
α-helix162-17110
α-helix176-1794
α-helix180-19011
α-helix199-2013
α-helix202-2076
α-helix208-22417
α-helix226-2283
α-helix231-2377
β-strand243-24423
β-strand24714
β-strand25214
β-strand256-25723
α-helix260-2634
α-helix267-2715
α-helix275-28612
β-strand28815
α-helix2961
β-strand29715
α-helix2981
α-helix300-31112
α-helix314-3196
α-helix320-3278
α-helix345-36117
β-strand36316
β-strand36916
α-helix370-38314
β-strand392-39437
α-helix397-40610
α-helix412-42211
α-helix446-4483
β-strand450-45237
α-helix453-46513
α-helix475-48410
α-helix487-50620
α-helix513-5153
α-helix517-5193
α-helix520-54122
α-helix554-5563
α-helix559-57214
α-helix575-58612
α-helix589-5902
β-strand595-59732
α-helix611-6133
α-helix614-6174
β-strand619-62462
β-strand627-63372
α-helix643-6486
β-strand650-661122
α-helix665-6739
α-helix679-6824
α-helix686-6949
α-helix701-7044
α-helix714-73017
α-helix734-7374
α-helix741-7433
α-helix744-7463
α-helix750-76011
β-strand762-76982
α-helix771-7799
β-strand783-78972
α-helix791-7933
α-helix800-8023
α-helix803-81210
α-helix814-8185
β-strand822-82432
β-strand829-83352
β-strand84318
β-strand849-85029
β-strand860-86129
β-strand86718
α-helix871-8744
β-strand877-886102
α-helix896-90611
α-helix908-9103
β-strand912-917610
β-strand925-929510
β-strand935-940610
β-strand943-944211
β-strand951-952211
α-helix953-96816
α-helix972-9743
α-helix977-99923
β-strand1001-1006610
α-helix1019-103618
β-strand103811
β-strand1048112
β-strand1053112
β-strand105511
α-helix1059-10613
α-helix1065-10673
β-strand1070-1071210
β-strand1074-1077410
α-helix1102-11109
β-strand1114-1118513
β-strand1123-1129713
α-helix1130-11323
β-strand1141-1145513
β-strand1150-1153414
β-strand1165-1168414
α-helix1170-118011
β-strand1190113
α-helix1192-11976
α-helix1201-121414
β-strand1218-1219215
β-strand1228-1229215
β-strand1230-1234516
β-strand1240-1242316
α-helix1254-127522
α-helix1281-12822
α-helix1285-12873
α-helix1288-129710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CRISPR-associated endonuclease Cpf1Aprotein1302Francisella tularensis subsp. novicida (strain U112)A0Q7Q2 (AlphaFold model)
pre-crRNABNA-hybrid46synthetic construct
DNA target strandCDNA38synthetic construct
DNA non-target strandDDNA38synthetic construct
Sequence of entity 1 (A), FASTA
>5NFV_1 CRISPR-associated endonuclease Cpf1 (chains A)
SNASIYQEFVNKYSLSKTLRFELIPQGKTLENIKARGLILDDEKRAKDYKKAKQIIDKYH
QFFIEEILSSVCISEDLLQNYSDVYFKLKKSDDDNLQKDFKSAKDTIKKQISEYIKDSEK
FKNLFNQNLIDAKKGQESDLILWLKQSKDNGIELFKANSDITDIDEALEIIKSFKGWTTY
FKGFHENRKNVYSSNDIPTSIIYRIVDDNLPKFLENKAKYESLKDKAPEAINYEQIKKDL
AEELTFDIDYKTSEVNQRVFSLDEVFEIANFNNYLNQSGITKFNTIIGGKFVNGENTKRK
GINEYINLYSQQINDKTLKKYKMSVLFKQILSDTESKSFVIDKLEDDSDVVTTMQSFYEQ
IAAFKTVEEKSIKETLSLLFDDLKAQKLDLSKIYFKNDKSLTDLSQQVFDDYSVIGTAVL
EYITQQIAPKNLDNPSKKEQELIAKKTEKAKYLSLETIKLALEEFNKHRDIDKQCRFEEI
LANFAAIPMIFDEIAQNKDNLAQISIKYQNQGKKDLLQASAEDDVKAIKDLLDQTNNLLH
KLKIFHISQSEDKANILDKDEHFYLVFEECYFELANIVPLYNKIRNYITQKPYSDEKFKL
NFENSTLANGWDKNKEPDNTAILFIKDDKYYLGVMNKKNNKIFDDKAIKENKGEGYKKIV
YKLLPGANKMLPKVFFSAKSIKFYNPSEDILRIRNHSTHTKNGSPQKGYEKFEFNIEDCR
KFIDFYKQSISKHPEWKDFGFRFSDTQRYNSIDEFYREVENQGYKLTFENISESYIDSVV
NQGKLYLFQIYNKDFSAYSKGRPNLHTLYWKALFDERNLQDVVYKLNGEAELFYRKQSIP
KKITHPAKEAIANKNKDNPKKESVFEYDLIKDKRFTEDKFFFHCPITINFKSSGANKFND
EINLLLKEKANDVHILSIDRGERHLAYYTLVDGKGNIIKQDTFNIIGNDRMKTNYHDKLA
AIEKDRDSARKDWKKINNIKEMKEGYLSQVVHEIAKLVIEYNAIVVFQDLNFGFKRGRFK
VEKQVYQKLEKMLIEKLNYLVFKDNEFDKTGGVLRAYQLTAPFETFKKMGKQTGIIYYVP
AGFTSKICPVTGFVNQLYPKYESVSKSQEFFSKFDKICYNLDKGYFEFSFDYKNFGDKAA
KGKWTIASFGSRLINFRNSDKNHNWDTREVYPTKELEKLLKDYSIEYGHGECIKAAICGE
SDKKFFAKLTSVLNTILQMANSKTGTELDYLISPVADVNGNFFDSRQAPKNMPQDADANG
AYHIGLKGLMLLGRIKNNQEGKKLNLVIKNEEYFEFVQNRNN
Sequence of entity 2 (B), FASTA
>5NFV_2 pre-crRNA (chains B)
AAUAAUUUCUACUGUUGUAGAUAGAUUAAAAGGUAAUUCUAUCUUG
Sequence of entity 3 (C), FASTA
>5NFV_3 DNA target strand (chains C)
ATAGTTCATAGAATTACCTTTTAATCTTAAAGGACTGC
Sequence of entity 4 (D), FASTA
>5NFV_4 DNA non-target strand (chains D)
AGTCCTTTATCTAATTTTCCATTAAGATAGAACTATGC

Ligands and cofactors

IDNameFormulaCopies
B3P2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-pr…C11 H26 N2 O61
MGMagnesium ionMg3

Primary citation

Structural Basis for Guide RNA Processing and Seed-Dependent DNA Targeting by CRISPR-Cas12a. Swarts, D.C., van der Oost, J., Jinek, M. Mol Cell (2017) 66:221-233.e4. DOI 10.1016/j.molcel.2017.03.016 · 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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