9JTS: Mouse RAG SEC-1DNA

CryoEM structure of mouse RAG SEC-1DNA (12RSS side). Determined by electron microscopy at 3.36 Å resolution. Released 23 Jul 2025.

Method: Electron microscopy
Resolution: 3.36 Å
Organisms: Mus musculus, Escherichia coli
Chains: 10
Atoms: 18,706
Mol. weight: 407.66 kDa
Ligands: CA, ZN
Released: 23 Jul 2025

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

Secondary structure: helices and β-sheets

9JTS contains 77 α-helices and 98 β-strands across 4 chains. 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: 28 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	409-418	10
α-helix	419-423	5
α-helix	428-442	15
α-helix	445-455	11
α-helix	464-473	10
α-helix	478-492	15
α-helix	500-506	7
β-strand	517-519	3	1
α-helix	522-523	2
β-strand	535-536	2	1
β-strand	554-556	3	1
α-helix	559-569	11
α-helix	571-580	10
β-strand	590-602	13	1
α-helix	605-608	4
β-strand	619-633	15	1
β-strand	636-642	7	1
β-strand	653-658	6	1
α-helix	665-682	18
β-strand	687-691	5	1
β-strand	694-707	14	1
α-helix	709-715	7
β-strand	725	1	2
β-strand	733	1	2
α-helix	734-740	7
α-helix	750-762	13
α-helix	769-776	8
α-helix	793-811	19
α-helix	823-841	19
α-helix	851-857	7
α-helix	860-867	8
α-helix	874-889	16
α-helix	890-892	3
α-helix	903-923	21
α-helix	934-941	8
α-helix	943-950	8
α-helix	959-974	16
α-helix	983-995	13
α-helix	1005-1007	3

Chain B: 8 helices, 38 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	3
α-helix	12-14	3
β-strand	15-24	10	4
β-strand	27-33	7	4
β-strand	46-47	2	4
β-strand	50	1	5
β-strand	55	1	5
β-strand	59	1	4
β-strand	61	1	6
β-strand	77-80	4	6
β-strand	90-97	8	6
β-strand	103-116	14	6
β-strand	119-127	9	6
β-strand	130-131	2	7
α-helix	133-136	4
β-strand	138	1	8
β-strand	142-147	6	7
β-strand	150-155	6	7
β-strand	159-161	3	8
α-helix	162-163	2
α-helix	169-171	3
β-strand	175-177	3	8
α-helix	178-179	2
α-helix	181	1
β-strand	182-186	5	7
β-strand	191-195	5	7
β-strand	205	1	9
β-strand	208-211	4	10
β-strand	215-219	5	10
β-strand	222	1	9
β-strand	223	1	11
β-strand	228	1	11
β-strand	233-239	7	10
β-strand	246-251	6	10
β-strand	259	1	12
β-strand	262-267	6	13
β-strand	270-274	5	13
β-strand	277	1	12
β-strand	283	1	12
β-strand	288-292	5	13
β-strand	297-301	5	13
α-helix	303-305	3
α-helix	309-312	4
β-strand	318-321	4	3
β-strand	326-332	7	3
β-strand	343-349	7	3

Chain C: 34 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	396-398	3
α-helix	401-407	7
α-helix	411-422	12
α-helix	427-442	16
α-helix	445-456	12
α-helix	464-473	10
α-helix	478-492	15
α-helix	498-499	2
α-helix	500-507	8
β-strand	517-519	3	14
α-helix	522-523	2
β-strand	535-536	2	14
β-strand	554-556	3	14
α-helix	559-569	11
α-helix	571-580	10
α-helix	589-590	2
β-strand	591-601	11	14
α-helix	605-608	4
β-strand	620-632	13	14
β-strand	637-642	6	14
β-strand	653-658	6	14
α-helix	666-682	17
β-strand	687-691	5	14
β-strand	694-706	13	14
α-helix	709-715	7
β-strand	725	1	15
β-strand	733	1	15
α-helix	734-739	6
α-helix	751-762	12
α-helix	769-776	8
α-helix	793-811	19
α-helix	823-840	18
α-helix	851-857	7
α-helix	860-866	7
α-helix	867-869	3
α-helix	873-894	22
α-helix	903-907	5
α-helix	909-923	15
α-helix	934-941	8
α-helix	943-949	7
α-helix	954-956	3
α-helix	959-974	16
α-helix	984-994	11
α-helix	997-1000	4
α-helix	1001-1003	3

Chain D: 7 helices, 38 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	16
β-strand	7-8	2	17
α-helix	12-14	3
β-strand	15-24	10	17
β-strand	27-33	7	17
β-strand	46-51	6	17
β-strand	54-59	6	17
β-strand	61-62	2	18
β-strand	77-78	2	19
β-strand	91-97	7	19
β-strand	103-110	8	19
β-strand	112-116	5	18
β-strand	119-122	4	18
β-strand	125-127	3	19
β-strand	130-131	2	20
α-helix	133-136	4
β-strand	138	1	21
β-strand	142-147	6	20
β-strand	150-155	6	20
β-strand	159-161	3	21
α-helix	162-163	2
α-helix	169-171	3
β-strand	175-177	3	21
α-helix	178-179	2
β-strand	182-186	5	20
β-strand	191-195	5	20
β-strand	205	1	22
β-strand	208-210	3	23
β-strand	215-219	5	23
β-strand	222	1	22
β-strand	223	1	24
β-strand	228	1	24
β-strand	233-239	7	23
β-strand	246-251	6	23
β-strand	259	1	25
β-strand	262-267	6	26
β-strand	270-274	5	26
β-strand	277	1	25
β-strand	287-291	5	26
β-strand	298-302	5	26
α-helix	303-305	3
α-helix	309-313	5
β-strand	318-321	4	16
β-strand	326-332	7	16
β-strand	343-349	7	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
V(D)J recombination-activating protein 1	A, C	protein	1040	Mus musculus	P15919 (AlphaFold model)
V(D)J recombination-activating protein 2	B, D	protein	527	Mus musculus	P21784 (AlphaFold model)
DNA (5'-d(ptpgpgpaptpcptpgpgpcpcptp*g)-3')	I	DNA	13	Escherichia coli
DNA (39-mer)	G	DNA	39	Escherichia coli
DNA (30-mer)	L	DNA	30	Escherichia coli
DNA (39-mer)	M	DNA	39	Escherichia coli
DNA (5'-d(cpapgpgpcpcpapgpaptpcpcp*a)-3')	H	DNA	13	Escherichia coli
DNA (30-mer)	F	DNA	30	Escherichia coli

Sequence of entity 1 (A, C), FASTA

>9JTS_1 V(D)J recombination-activating protein 1 (chains A, C)
MAASLPSTLSFSSAPDEIQHPQIKFSEWKFKLFRVRSFEKAPEEAQKEKDSSEGKPYLEQ
SPVVPEKPGGQNSILTQRALKLHPKFSKKFHADGKSSDKAVHQARLRHFCRICGNRFKSD
GHSRRYPVHGPVDAKTQSLFRKKEKRVTSWPDLIARIFRIDVKADVDSIHPTEFCHDCWS
IMHRKFSSSHSQVYFPRKVTVEWHPHTPSCDICFTAHRGLKRKRHQPNVQLSKKLKTVLN
HARRDRRKRTQARVSSKEVLKKISNCSKIHLSTKLLAVDFPAHFVKSISCQICEHILADP
VETSCKHLFCRICILRCLKVMGSYCPSCRYPCFPTDLESPVKSFLNILNSLMVKCPAQDC
NEEVSLEKYNHHVSSHKESKETLVHINKGGRPRQHLLSLTRRAQKHRLRELKIQVKEFAD
KEEGGDVKAVCLTLFLLALRARNEHRQADELEAIMQGRGSGLQPAVCLAIRVNTFLSCSQ
YHKMYRTVKAITGRQIFQPLHALRNAEKVLLPGYHPFEWQPPLKNVSSRTDVGIIDGLSG
LASSVDEYPVDTIAKRFRYDSALVSALMDMEEDILEGMRSQDLDDYLNGPFTVVVKESCD
GMGDVSEKHGSGPAVPEKAVRFSFTVMRITIEHGSQNVKVFEEPKPNSELCCKPLCLMLA
DESDHETLTAILSPLIAEREAMKSSELTLEMGGIPRTFKFIFRGTGYDEKLVREVEGLEA
SGSVYICTLCDTTRLEASQNLVFHSITRSHAENLQRYEVWRSNPYHESVEELRDRVKGVS
AKPFIETVPSIDALHCDIGNAAEFYKIFQLEIGEVYKHPNASKEERKRWQATLDKHLRKR
MNLKPIMRMNGNFARKLMTQETVDAVCELIPSEERHEALRELMDLYLKMKPVWRSSCPAK
ECPESLCQYSFNSQRFAELLSTKFKYRYEGKITNYFHKTLAHVPEIIERDGSIGAWASEG
NESGNKLFRRFRKMNARQSKCYEMEDVLKHHWLYTSKYLQKFMNAHNALKSSGFTMNSKE
TLGDPLGIEDSLESQDSMEF

Sequence of entity 2 (B, D), FASTA

>9JTS_2 V(D)J recombination-activating protein 2 (chains B, D)
MSLQMVTVGHNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHFDIKQNHLKLKPA
IFSKDSCYLPPLRYPATCSYKGSIDSDKHQYIIHGGKTPNNELSDKIYIMSVACKNNKKV
TFRCTEKDLVGDVPEPRYGHSIDVVYSRGKSMGVLFGGRSYMPSTQRTTEKWNSVADCLP
HVFLIDFEFGCATSYILPELQDGLSFHVSIARNDTVYILGGHSLASNIRPANLYRIRVDL
PLGTPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMVCSLVSLGDNTIEIS
EMETPDWTSDIKHSKIWFGSNMGNGTIFLGIPGDNKQAMSEAFYFYTLRCSEEDLSEDQK
IVSNSQTSTEDPGDSTPFEDSEEFCFSAEATSFDGDDEFDTYNEDDEDDESVTGYWITCC
PTCDVDINTWVPFYSTELNKPAMIYCSHGDGHWVHAQCMDLEERTLIHLSEGSNKYYCNE
HVQIARALQTPKRNPPLQKPPMKSLHKKGSGKVLTPAKKSFLRRLFD

Sequence of entity 3 (I), FASTA

>9JTS_3 DNA (5'-D(P*TP*GP*GP*AP*TP*CP*TP*GP*GP*CP*CP*TP*G)-3') (chains I)
TGGATCTGGCCTG

Sequence of entity 4 (G), FASTA

>9JTS_4 DNA (39-MER) (chains G)
GGTTTTTGTCTGGCTTCACACTTGATTTGCATCACTGTG

Sequence of entity 5 (L), FASTA

>9JTS_5 DNA (30-MER) (chains L)
CACAGTGATACAGCCCTTAACAAAAACCCG

Sequence of entity 6 (M), FASTA

>9JTS_6 DNA (39-MER) (chains M)
CACAGTGATGCAAATCAAGTGTGAAGCCAGACAAAAACC

Sequence of entity 7 (H), FASTA

>9JTS_7 DNA (5'-D(*CP*AP*GP*GP*CP*CP*AP*GP*AP*TP*CP*CP*A)-3') (chains H)
CAGGCCAGATCCA

Sequence of entity 8 (F), FASTA

>9JTS_8 DNA (30-MER) (chains F)
CGGGTTTTTGTTAAGGGCTGTATCACTGTG

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
ZN	Zinc ion	Zn	2

Primary citation

How RAG1/2 evolved from ancestral transposases to initiate V(D)J recombination without transposition. Chen, X., Yao, L., Li, W. et al. Proc Natl Acad Sci U S A (2025) 122:e2512362122-e2512362122. DOI 10.1073/pnas.2512362122 · PubMed

Other PDB entries of the same protein (UniProt P15919 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RMD 2.1 Å, RAG1 dimerization domain
3GNA 2.4 Å, Crystal structure of the RAG1 nonamer-binding domain with DNA
6XNX 2.7 Å, Structure of RAG1 (R848M/E649V)-RAG2-DNA Strand Transfer Complex (Dynamic-Form)
5ZE0 2.75 Å, Hairpin Forming Complex, RAG1/2-Nicked(with Dideoxy) 12RSS/23RSS complex in Mg2+
5ZDZ 2.8 Å, Hairpin Forming Complex, RAG1/2-Nicked 12RSS/23RSS complex in Ca2+
6XNY 2.9 Å, Structure of RAG1 (R848M/E649V)-RAG2-DNA Strand Transfer Complex (Paired-Form)
9JPX 2.95 Å, CryoEM structure of mouse RAG SEC-0
3GNB 3.0 Å, Crystal structure of the RAG1 nonamer-binding domain with DNA
5ZE1 3.0 Å, Hairpin Forming Complex, RAG1/2-Nicked 12RSS/23RSS complex in 2mM Mn2+ for 10 min at 4'C
9LQO 3.0 Å, Structure of RAG transposon end complex (TEC)
9JQN 3.03 Å, CryoEM structure of mouse RAG SEC-2DNA
6OES 3.06 Å, Cryo-EM structure of mouse RAG1/2 STC complex (without NBD domain)

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