9WSR: Mouse NLRP14-KDM2A-SKP1 complex

Structure of mouse NLRP14-KDM2A-SKP1 complex. Determined by electron microscopy at 2.79 Å resolution. Released 18 Mar 2026.

Method: Electron microscopy
Resolution: 2.79 Å
Organism: Mus musculus
Chains: 3
Atoms: 9,408
Mol. weight: 176.51 kDa
Released: 18 Mar 2026

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

Secondary structure: helices and β-sheets

9WSR contains 68 α-helices and 39 β-strands across 3 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: 41 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	235-245	11
α-helix	252-260	9
α-helix	263-267	5
α-helix	272-288	17
α-helix	293-296	4
α-helix	299-309	11
α-helix	320-323	4
α-helix	324-340	17
β-strand	344-346	3	4
α-helix	347-352	6
α-helix	357-365	9
β-strand	369-371	3	4
β-strand	378-381	4	4
α-helix	384-397	14
α-helix	407-409	3
α-helix	414-418	5
α-helix	429-437	9
α-helix	441-451	11
α-helix	458-469	12
α-helix	476-490	15
α-helix	495-500	6
β-strand	507-514	8	5
α-helix	515-525	11
β-strand	533-538	6	5
β-strand	539	1	6
β-strand	540-543	4	5
α-helix	551-553	3
α-helix	556-568	13
α-helix	569-571	3
β-strand	579-583	5	5
β-strand	586-587	2	6
α-helix	589-599	11
β-strand	608-612	5	5
β-strand	615-616	2	6
α-helix	624-627	4
β-strand	634-638	5	5
α-helix	644-655	12
β-strand	663-667	5	5
α-helix	673-683	11
β-strand	691-693	3	5
α-helix	701-711	11
β-strand	720-722	3	5
α-helix	730-732	3
α-helix	733-742	10
β-strand	748-750	3	5
α-helix	758-768	11
β-strand	777-779	3	5
α-helix	787-796	10
α-helix	797-799	3
β-strand	805-807	3	5
α-helix	815-825	11
β-strand	834-836	3	5
α-helix	844-846	3
α-helix	847-856	10
β-strand	864	1	5
α-helix	872-882	11
β-strand	891-893	3	5
α-helix	901-903	3
α-helix	904-913	10
β-strand	919-921	3	5
α-helix	929-939	11
β-strand	948-950	3	5
α-helix	953-956	4
α-helix	959-971	13
β-strand	976-978	3	5

Chain B: 14 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	891-901	11
α-helix	906-912	7
α-helix	917-923	7
β-strand	931-933	3	1
α-helix	942-951	10
β-strand	955-957	3	1
α-helix	965-972	8
β-strand	980-982	3	1
β-strand	987	1	2
α-helix	988-991	4
α-helix	992-995	4
β-strand	1004-1006	3	1
β-strand	1011	1	2
α-helix	1015-1022	8
β-strand	1042-1044	3	1
α-helix	1052-1061	10
β-strand	1067-1069	3	1
α-helix	1078-1084	7
α-helix	1091-1094	4
β-strand	1097-1099	3	1
α-helix	1110-1113	4
α-helix	1114-1116	3
β-strand	1122-1124	3	1
α-helix	1133-1143	11
β-strand	1149-1151	3	1
β-strand	1156-1159	4	1

Chain C: 13 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	3
β-strand	13-17	5	3
α-helix	18-21	4
α-helix	25-33	9
α-helix	43-44	2
β-strand	45	1	3
α-helix	46	1
α-helix	52-64	13
α-helix	69-72	4
α-helix	76-79	4
α-helix	87-92	6
α-helix	97-109	13
α-helix	113-125	13
α-helix	132-139	8
α-helix	147-156	10
α-helix	158-162	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lysine-specific demethylase 2A	B	protein	358	Mus musculus	P59997 (AlphaFold model)
S-phase kinase-associated protein 1	C	protein	174	Mus musculus	Q9WTX5 (AlphaFold model)
NACHT, LRR and PYD domains-containing protein 14	A	protein	1013	Mus musculus	Q6B966 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>9WSR_1 Lysine-specific demethylase 2A (chains B)
MWSHPQFEKGTIVPKLQAITASSANLRPNPRVLMQHCPARNPQHGDEEGLGGEEEEEEEE
EEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMSVFRYLSRKELCECMRVCKTWYKWC
CDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLSWTNISKKQLTWLVNRLPGLKDLLL
AGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIRDLLTPPTDKPGQDNRSKLRNMTDF
RLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQSSNLLTAVGSSTRYSLTELNMAGC
NKLTDQTLFFLRRIANVTLIDLRGCKQITRKACEHFISDLSINSLYCLSDEKLIQKIS

Sequence of entity 2 (C), FASTA

>9WSR_2 S-phase kinase-associated protein 1 (chains C)
MWSHPQFEKGTMPTIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPN
VNAAILKKVIQWCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANY
LDIKGLLDVTCKTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK

Sequence of entity 3 (A), FASTA

>9WSR_3 NACHT, LRR and PYD domains-containing protein 14 (chains A)
MDYKDDDDKGDYKDDDDKGSMKTEDDEMEYEASKEETVSEDKDFDDGIDYRTVIKENIFT
MWYKTSLHGEFATLNCVITPKDQNLLQHIFDEDIQTSEAPQTVVLQGAAGIGKTTLLKKA
VLEWADGNLYQQFTHVFYLNGKEISQVKEKSFAQLISKHWPSSEGPIEQVLSKPSSLLFI
IDSFDELDFSFEEPQFALCKDWTQISPVSFLISSLLRKVMLPESYLLVATRSTAWKRLVP
LLQKPQRVKLSGLSKNARMDYIHHLLKDKAWATSAIYSLRMNWRLFHMCHVCHMCQMICA
VLKGQVEKGGRVEETCKTSTALFTYYICSLFPRIPVGCVTLPNETLLRSLCKAAVEGIWT
MKHVLYQQNLRKHELTREDILLFLDAKVLQQDTEYENCYMFTHLHVQEFFAALFYLLREN
LEEQDYPSEPFENLYLLLESNHIHDPHLEQMKCFLFGLLNKDRVRQLEETFNLTISMEVR
EELLACLEGLEKDDSSLSQLRFQDLLHCIYETQDQEFITQALMYFQKIIVRVDEEPQLRI
YSFCLKHCHTLKTMRLTARADLKNMLDTAEMCLEGAAVQVIHYWQDLFSVLHTNESLIEM
DLYESRLDESLMKILNEELSHPKCKLQKLIFRAVDFLNGCQDFTFLASNKKVTHLDLKET
DLGVNGLKTLCEALKCKGCKLRVLRLASCDLNVARCQKLSNALQTNRSLVFLNLSLNNLS
NDGVKSLCEVLENPNSSLERLALASCGLTKAGCKVLSSALTKSKRLTHLCLSDNVLEDEG
IKLLSHTLKHPQCTLQSLVLRSCSFTPIGSEHLSTALLHNRSLVHLDLGQNKLADNGVKL
LCHSLQQPHCNLQELELMSCVLTSKACGDLASVLVNNSNLWSLDLGHNILDDAGLNILCD
ALRNPNCHVQRLGLENCGLTPGCCQDLLGILSNNKSVIQMNLMKNALDHESIKNLCKVLR
SPTCKMEFLALDKKEILKKKIKKFLVDVRINNPHLVIGPECPNTESGCWWNYF

Primary citation

NLRP14 modulates the activity of E3 ubiquitin ligases during the oocyte-to-embryo transition. Liu, S., Qi, Q., Chi, P. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-71519-4 · PubMed

Other PDB entries of the same protein (UniProt P59997 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4QXB 1.6 Å, crystal structure of histone demethylase KDM2A-H3K36ME3 with NOG
4QX8 1.65 Å, Crystal structure of histone demethylase kdm2a-h3k36me3 complex with alpha-kg
4QXC 1.75 Å, Crystal structure of histone demethylase KDM2A-H3K36ME2 with NOG
7UVA 1.98 Å, Crystal structure of KDM2A histone demethylase catalytic domain in complex with an H3C36…
4QWN 2.1 Å, Histone demethylase KDM2A-H3K36ME1-alpha-KG complex structure
4QXH 2.2 Å, Crystal structure of histone demethylase KDM2A-H3K36ME1 with NOG
4TN7 2.2 Å, Crystal structure of mouse KDM2A-H3K36ME-NO complex
4QX7 2.34 Å, Crystal structure of histone demethylase kdm2a-h3k36me2 with alpha-kg
9WSQ 3.35 Å, Structure of dimeric mouse NLRP14-KDM2A-SKP1 complex

Browse structure collections

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