9WSQ: Dimeric mouse NLRP14-KDM2A-SKP1 complex

Structure of dimeric mouse NLRP14-KDM2A-SKP1 complex. Determined by electron microscopy at 3.35 Å resolution. Released 18 Mar 2026.

Method
Electron microscopy
Resolution
3.35 Å
Organism
Mus musculus
Chains
6
Atoms
18,805
Mol. weight
352.75 kDa
Released
18 Mar 2026

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

Secondary structure: helices and β-sheets

9WSQ contains 136 α-helices and 78 β-strands across 6 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.

Chains A and D: 41 helices, 24 β-strands

ElementResiduesLengthSheet
α-helix235-24511
α-helix252-2609
α-helix263-2675
α-helix268-2703
α-helix272-28817
α-helix299-30911
α-helix320-3234
α-helix324-34017
β-strand345-34624
α-helix347-3526
α-helix357-3659
β-strand369-37134
β-strand378-38144
α-helix384-39714
α-helix407-4093
α-helix414-4185
α-helix429-4379
α-helix441-45111
α-helix459-46810
α-helix476-49015
α-helix495-5006
β-strand507-51485
α-helix515-52511
β-strand533-53865
β-strand53916
β-strand540-54345
α-helix551-5533
α-helix556-56712
α-helix568-5714
β-strand579-58355
β-strand586-58726
α-helix589-59911
β-strand608-61255
β-strand615-61626
α-helix624-6274
β-strand634-63855
α-helix644-65512
β-strand663-66755
α-helix673-68311
β-strand691-69335
α-helix701-71111
β-strand720-72235
α-helix730-7323
α-helix733-74210
β-strand748-75035
α-helix758-76811
β-strand777-77935
α-helix787-79610
α-helix797-7993
β-strand805-80735
α-helix815-82511
β-strand834-83635
α-helix844-8463
α-helix847-85610
β-strand86415
α-helix872-88211
β-strand891-89335
α-helix901-9033
α-helix904-91310
β-strand919-92135
α-helix929-93911
β-strand948-95035
α-helix953-9564
α-helix959-97113
β-strand976-97835
Chains B and E: 14 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix891-90111
α-helix906-9127
α-helix917-9237
β-strand931-93331
α-helix942-95110
β-strand955-95731
α-helix965-9728
β-strand980-98231
β-strand98712
α-helix988-9914
α-helix992-9954
β-strand1004-100631
β-strand101112
α-helix1015-10228
β-strand1042-104431
α-helix1052-106110
β-strand1067-106931
α-helix1078-10847
α-helix1091-10944
β-strand1097-109931
α-helix1110-11134
α-helix1114-11163
β-strand1122-112431
α-helix1133-114311
β-strand1149-115131
β-strand1156-115941
Chains C and F: 13 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand3-753
β-strand13-1753
α-helix18-214
α-helix25-339
α-helix43-442
β-strand4513
α-helix461
α-helix52-6413
α-helix69-724
α-helix76-794
α-helix87-926
α-helix97-10913
α-helix113-12513
α-helix132-1398
α-helix147-15610
α-helix158-1625

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lysine-specific demethylase 2AB, Eprotein358Mus musculusP59997 (AlphaFold model)
S-phase kinase-associated protein 1C, Fprotein174Mus musculusQ9WTX5 (AlphaFold model)
NACHT, LRR and PYD domains-containing protein 14A, Dprotein1012Mus musculusQ6B966 (AlphaFold model)
Sequence of entity 1 (B, E), FASTA
>9WSQ_1 Lysine-specific demethylase 2A (chains B, E)
MWSHPQFEKGTIVPKLQAITASSANLRPNPRVLMQHCPARNPQHGDEEGLGGEEEEEEEE
EEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMSVFRYLSRKELCECMRVCKTWYKWC
CDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLSWTNISKKQLTWLVNRLPGLKDLLL
AGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIRDLLTPPTDKPGQDNRSKLRNMTDF
RLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQSSNLLTAVGSSTRYSLTELNMAGC
NKLTDQTLFFLRRIANVTLIDLRGCKQITRKACEHFISDLSINSLYCLSDEKLIQKIS
Sequence of entity 2 (C, F), FASTA
>9WSQ_2 S-phase kinase-associated protein 1 (chains C, F)
MWSHPQFEKGTMPTIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPN
VNAAILKKVIQWCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANY
LDIKGLLDVTCKTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Sequence of entity 3 (A, D), FASTA
>9WSQ_3 NACHT, LRR and PYD domains-containing protein 14 (chains A, D)
DYKDDDDKGDYKDDDDKGSMKTEDDEMEYEASKEETVSEDKDFDDGIDYRTVIKENIFTM
WYKTSLHGEFATLNCVITPKDQNLLQHIFDEDIQTSEAPQTVVLQGAAGIGKTTLLKKAV
LEWADGNLYQQFTHVFYLNGKEISQVKEKSFAQLISKHWPSSEGPIEQVLSKPSSLLFII
DSFDELDFSFEEPQFALCKDWTQISPVSFLISSLLRKVMLPESYLLVATRSTAWKRLVPL
LQKPQRVKLSGLSKNARMDYIHHLLKDKAWATSAIYSLRMNWRLFHMCHVCHMCQMICAV
LKGQVEKGGRVEETCKTSTALFTYYICSLFPRIPVGCVTLPNETLLRSLCKAAVEGIWTM
KHVLYQQNLRKHELTREDILLFLDAKVLQQDTEYENCYMFTHLHVQEFFAALFYLLRENL
EEQDYPSEPFENLYLLLESNHIHDPHLEQMKCFLFGLLNKDRVRQLEETFNLTISMEVRE
ELLACLEGLEKDDSSLSQLRFQDLLHCIYETQDQEFITQALMYFQKIIVRVDEEPQLRIY
SFCLKHCHTLKTMRLTARADLKNMLDTAEMCLEGAAVQVIHYWQDLFSVLHTNESLIEMD
LYESRLDESLMKILNEELSHPKCKLQKLIFRAVDFLNGCQDFTFLASNKKVTHLDLKETD
LGVNGLKTLCEALKCKGCKLRVLRLASCDLNVARCQKLSNALQTNRSLVFLNLSLNNLSN
DGVKSLCEVLENPNSSLERLALASCGLTKAGCKVLSSALTKSKRLTHLCLSDNVLEDEGI
KLLSHTLKHPQCTLQSLVLRSCSFTPIGSEHLSTALLHNRSLVHLDLGQNKLADNGVKLL
CHSLQQPHCNLQELELMSCVLTSKACGDLASVLVNNSNLWSLDLGHNILDDAGLNILCDA
LRNPNCHVQRLGLENCGLTPGCCQDLLGILSNNKSVIQMNLMKNALDHESIKNLCKVLRS
PTCKMEFLALDKKEILKKKIKKFLVDVRINNPHLVIGPECPNTESGCWWNYF

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:

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