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8SXN

Structure of NLRP3 and NEK7 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000922cellular_componentspindle pole
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005815cellular_componentmicrotubule organizing center
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006468biological_processprotein phosphorylation
A0007346biological_processregulation of mitotic cell cycle
A0009306biological_processprotein secretion
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0032206biological_processpositive regulation of telomere maintenance
A0032731biological_processpositive regulation of interleukin-1 beta production
A0032741biological_processpositive regulation of interleukin-18 production
A0033044biological_processregulation of chromosome organization
A0035655biological_processinterleukin-18-mediated signaling pathway
A0035865biological_processcellular response to potassium ion
A0044546biological_processNLRP3 inflammasome complex assembly
A0046872molecular_functionmetal ion binding
A0050729biological_processpositive regulation of inflammatory response
A0051225biological_processspindle assembly
A0051604biological_processprotein maturation
A0070269biological_processpyroptotic inflammatory response
A0070498biological_processinterleukin-1-mediated signaling pathway
A0106310molecular_functionprotein serine kinase activity
A0140677molecular_functionmolecular function activator activity
A1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
B0000166molecular_functionnucleotide binding
B0000922cellular_componentspindle pole
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005815cellular_componentmicrotubule organizing center
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006468biological_processprotein phosphorylation
B0007346biological_processregulation of mitotic cell cycle
B0009306biological_processprotein secretion
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0032206biological_processpositive regulation of telomere maintenance
B0032731biological_processpositive regulation of interleukin-1 beta production
B0032741biological_processpositive regulation of interleukin-18 production
B0033044biological_processregulation of chromosome organization
B0035655biological_processinterleukin-18-mediated signaling pathway
B0035865biological_processcellular response to potassium ion
B0044546biological_processNLRP3 inflammasome complex assembly
B0046872molecular_functionmetal ion binding
B0050729biological_processpositive regulation of inflammatory response
B0051225biological_processspindle assembly
B0051604biological_processprotein maturation
B0070269biological_processpyroptotic inflammatory response
B0070498biological_processinterleukin-1-mediated signaling pathway
B0106310molecular_functionprotein serine kinase activity
B0140677molecular_functionmolecular function activator activity
B1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VmHrDIKpaNVFI
ChainResidueDetails
AVAL157-ILE169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:35254907, ECO:0000305|PubMed:36142182, ECO:0000305|PubMed:36442502, ECO:0007744|PDB:7VTP, ECO:0007744|PDB:7ZGU, ECO:0007744|PDB:8EJ4
ChainResidueDetails
CTHR169
DTHR169

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00136, ECO:0000269|PubMed:17483456, ECO:0000305|PubMed:34687713, ECO:0000305|PubMed:35114687, ECO:0000305|PubMed:35254907, ECO:0000305|PubMed:36142182, ECO:0000305|PubMed:36442502, ECO:0007744|PDB:7ALV, ECO:0007744|PDB:7PZC, ECO:0007744|PDB:7VTP, ECO:0007744|PDB:7ZGU, ECO:0007744|PDB:8EJ4
ChainResidueDetails
CGLY226
DGLY226
BILE40
BMET63

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:34687713, ECO:0000305|PubMed:35114687, ECO:0000305|PubMed:35254907, ECO:0000305|PubMed:36142182, ECO:0007744|PDB:7ALV, ECO:0007744|PDB:7PZC, ECO:0007744|PDB:7VTP, ECO:0007744|PDB:7ZGU
ChainResidueDetails
CHIS522
DHIS522

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by BTK => ECO:0000269|PubMed:34554188
ChainResidueDetails
CTYR136
CTYR140
CTYR143
CTYR168
DTYR136
DTYR140
DTYR143
DTYR168

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8R4B8
ChainResidueDetails
CSER161
CSER295
DSER161
DSER295

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:28943315
ChainResidueDetails
CSER163
CSER334
CSER728
CSER975
DSER163
DSER334
DSER728
DSER975

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK8 => ECO:0000269|PubMed:35114687
ChainResidueDetails
CSER198
DSER198

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:35114687
ChainResidueDetails
CSER201
DSER201

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by LATS1 and LATS2 => ECO:0000269|PubMed:39173637
ChainResidueDetails
CSER265
DSER265

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: Phosphoserine; by CSNK1A1 => ECO:0000269|PubMed:34615873
ChainResidueDetails
CSER735
CSER806
CSER1035
DSER735
DSER806
DSER1035

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:27043286
ChainResidueDetails
CTYR861
DTYR861

site_idSWS_FT_FI12
Number of Residues6
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:36586411
ChainResidueDetails
CCYS837
CCYS838
CCYS844
DCYS837
DCYS838
DCYS844

site_idSWS_FT_FI13
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:39173637
ChainResidueDetails
CCYS958
DCYS958

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:26037928
ChainResidueDetails
CLYS689
DLYS689

site_idSWS_FT_FI15
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:34615873
ChainResidueDetails
CLYS878
CLYS927
CLYS973
DLYS878
DLYS927
DLYS973

237735

PDB entries from 2025-06-18

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