9MKV: FnoCas12a bridge helix variant state 3

FnoCas12a bridge helix variant state 3. Determined by electron microscopy at 3.68 Å resolution. Released 11 Feb 2026.

Method
Electron microscopy
Resolution
3.68 Å
Organisms
Francisella tularensis subsp. novicida U112, synthetic construct
Chains
4
Atoms
8,481
Mol. weight
181 kDa
Released
11 Feb 2026

Explore 9MKV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9MKV contains 44 α-helices and 26 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: 44 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand811
β-strand13-22102
α-helix27-348
α-helix40-6829
α-helix74-785
α-helix84-885
α-helix94-11421
α-helix117-1204
α-helix125-1273
α-helix137-1426
α-helix162-1709
α-helix181-1899
α-helix199-2024
α-helix203-2075
α-helix208-22114
α-helix233-2375
α-helix266-2727
α-helix275-28612
α-helix300-3067
α-helix325-3273
β-strand595-59622
α-helix614-6174
β-strand620-62452
β-strand627-63372
α-helix644-6474
β-strand655-66172
α-helix669-6735
α-helix678-6803
α-helix686-6916
α-helix715-73016
α-helix735-7373
α-helix750-7589
β-strand762-76762
α-helix772-7809
β-strand783-78972
α-helix791-7933
α-helix803-8108
α-helix814-8185
β-strand822-82432
β-strand829-83352
β-strand877-886102
α-helix896-90712
α-helix908-9103
β-strand912-91873
β-strand924-92963
β-strand935-94063
α-helix979-99315
α-helix996-9994
β-strand1001-100663
α-helix1022-103514
β-strand103811
α-helix10441
β-strand105511
α-helix1059-10613
β-strand1070-107123
β-strand1074-107743
α-helix1103-11108
β-strand1115-111624
β-strand1125-112734
β-strand1143-114424
β-strand1150-115125
β-strand1167-116825
α-helix1170-118011
α-helix1192-11976
α-helix1201-121515
β-strand123016
β-strand124216
α-helix1243-12453
α-helix1254-127421
α-helix1288-129710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CRISPR-associated endonuclease Cas12aAprotein1305Francisella tularensis subsp. novicida U112A0Q7Q2 (AlphaFold model)
crRNABRNA43synthetic construct
Ts DNACDNA24synthetic construct
Nts DNADDNA24synthetic construct
Sequence of entity 1 (A), FASTA
>9MKV_1 CRISPR-associated endonuclease Cas12a (chains A)
GAASHMSIYQEFVNKYSLSKTLRFELIPQGKTLENIKARGLILDDEKRAKDYKKAKQIID
KYHQFFIEEILSSVCISEDLLQNYSDVYFKLKKSDDDNLQKDFKSAKDTIKKQISEYIKD
SEKFKNLFNQNLIDAKKGQESDLILWLKQSKDNGIELFKANSDITDIDEALEIIKSFKGW
TTYFKGFHENRKNVYSSNDIPTSIIYRIVDDNLPKFLENKAKYESLKDKAPEAINYEQIK
KDLAEELTFDIDYKTSEVNQRVFSLDEVFEIANFNNYLNQSGITKFNTIIGGKFVNGENT
KRKGINEYINLYSQQINDKTLKKYKMSVLFKQILSDTESKSFVIDKLEDDSDVVTTMQSF
YEQIAAFKTVEEKSIKETLSLLFDDLKAQKLDLSKIYFKNDKSLTDLSQQVFDDYSVIGT
AVLEYITQQIAPKNLDNPSKKEQELIAKKTEKAKYLSLETIKLALEEFNKHRDIDKQCRF
EEILANFAAIPMIFDEIAQNKDNLAQISIKYQNQGKKDLLQASAEDDVKAIKDLLDQTNN
LLHKLKIFHISQSEDKANILDKDEHFYLVFEECYFELANIVPLYNKIRNYITQKPYSDEK
FKLNFENSTLANGWDKNKEPDNTAILFIKDDKYYLGVMNKKNNKIFDDKAIKENKGEGYK
KIVYKLLPGANKMLPKVFFSAKSIKFYNPSEDILRIRNHSTHTKNGSPQKGYEKFEFNIE
DCRKFIDFYKQSISKHPEWKDFGFRFSDTQRYNSIDEFYREVENQGYKLTFENISESYID
SVVNQGKLYLFQIYNKDFSAYSKGRPNLHTLYWKALFDERNLQDVVYKLNGEAELFYRKQ
SIPKKITHPAKEAIANKNKDNPKKESVFEYDLIKDKRFTEDKFFFHCPITINFKSSGANK
FNDEINLLLKEKANDVHILSIDRGERHLAYYTLVDGKGNIIKQDTFNIIGNDRMKTNYHD
KLAAIEKDRDSARPPWKKINNIKEMKEGYLSQVVHEIAKLVIEYNAIVVFEDLNFGFKRG
RFKVEKQVYQKLEKMLIEKLNYLVFKDNEFDKTGGVLRAYQLTAPFETFKKMGKQTGIIY
YVPAGFTSKICPVTGFVNQLYPKYESVSKSQEFFSKFDKICYNLDKGYFEFSFDYKNFGD
KAAKGKWTIASFGSRLINFRNSDKNHNWDTREVYPTKELEKLLKDYSIEYGHGECIKAAI
CGESDKKFFAKLTSVLNTILQMRNSKTGTELDYLISPVADVNGNFFDSRQAPKNMPQDAD
ANGAYHIGLKGLMLLGRIKNNQEGKKLNLVIKNEEYFEFVQNRNN
Sequence of entity 2 (B), FASTA
>9MKV_2 crRNA (chains B)
AAUUUCUACUGUUGUAGAUGAGAAGUCAUUUAAUAAGGCCACU
Sequence of entity 3 (C), FASTA
>9MKV_3 TS DNA (chains C)
GCCTTATTAAATGACTTCTCTAAA
Sequence of entity 4 (D), FASTA
>9MKV_4 NTS DNA (chains D)
TTTAGAGAAGTCATTTAATAAGGC

Primary citation

Bridge helix of Cas12a is an allosteric regulator of R-loop formation and RuvC activation. Ganguly, C., Aribam, S.D., Dos Santos, A.M. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-68657-0 · 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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