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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6NPY

Cryo-EM structure of NLRP3 bound to NEK7

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0002221biological_processpattern recognition receptor signaling pathway
A0002376biological_processimmune system process
A0002674biological_processnegative regulation of acute inflammatory response
A0002830biological_processpositive regulation of type 2 immune response
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005815cellular_componentmicrotubule organizing center
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0006355biological_processregulation of DNA-templated transcription
A0006915biological_processapoptotic process
A0006952biological_processdefense response
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007231biological_processosmosensory signaling pathway
A0009306biological_processprotein secretion
A0009595biological_processdetection of biotic stimulus
A0009615biological_processresponse to virus
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031021cellular_componentinterphase microtubule organizing center
A0032691biological_processnegative regulation of interleukin-1 beta production
A0032731biological_processpositive regulation of interleukin-1 beta production
A0032741biological_processpositive regulation of interleukin-18 production
A0032753biological_processpositive regulation of interleukin-4 production
A0035591molecular_functionsignaling adaptor activity
A0035655biological_processinterleukin-18-mediated signaling pathway
A0042802molecular_functionidentical protein binding
A0042834molecular_functionpeptidoglycan binding
A0043531molecular_functionADP binding
A0043565molecular_functionsequence-specific DNA binding
A0044546biological_processNLRP3 inflammasome complex assembly
A0045087biological_processinnate immune response
A0045630biological_processpositive regulation of T-helper 2 cell differentiation
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0050727biological_processregulation of inflammatory response
A0050728biological_processnegative regulation of inflammatory response
A0050729biological_processpositive regulation of inflammatory response
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0051260biological_processprotein homooligomerization
A0051604biological_processprotein maturation
A0060090molecular_functionmolecular adaptor activity
A0061702cellular_componentcanonical inflammasome complex
A0070269biological_processpyroptotic inflammatory response
A0070273molecular_functionphosphatidylinositol-4-phosphate binding
A0070498biological_processinterleukin-1-mediated signaling pathway
A0071222biological_processcellular response to lipopolysaccharide
A0072559cellular_componentNLRP3 inflammasome complex
A0098586biological_processcellular response to virus
A0140297molecular_functionDNA-binding transcription factor binding
A0140299molecular_functionmolecular sensor activity
A0140608molecular_functioncysteine-type endopeptidase activator activity
A0140693molecular_functionmolecular condensate scaffold activity
A1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
A1901223biological_processnegative regulation of non-canonical NF-kappaB signal transduction
A1901224biological_processpositive regulation of non-canonical NF-kappaB signal transduction
A1901981molecular_functionphosphatidylinositol phosphate binding
A2000553biological_processpositive regulation of T-helper 2 cell cytokine production
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ADP A 1101
ChainResidue
AARG165
ATRP414
AHIS520
ATYR166
ATHR167
AGLY229
ALYS230
ATHR231
AILE232
ATYR379
ALEU411
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGQFSEVYrAacrldgkt..........VALK
ChainResidueDetails
BILE40-LYS63
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VmHrDIKpaNVFI
ChainResidueDetails
BVAL157-ILE169
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues21
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues20
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues21
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues20
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues21
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues20
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues21
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues21
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsMotif: {"description":"KFERQ-like motif 1","evidences":[{"source":"PubMed","id":"36586411","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsMotif: {"description":"KFERQ-like motif 3","evidences":[{"source":"PubMed","id":"36586411","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsMotif: {"description":"KFERQ-like motif 4","evidences":[{"source":"PubMed","id":"36586411","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35254907","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36142182","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36442502","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7VTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZGU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8EJ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00136","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17483456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34687713","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35114687","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35254907","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36142182","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36442502","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7ALV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PZC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7VTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZGU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8EJ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34687713","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35114687","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35254907","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36142182","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7ALV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PZC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7VTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZGU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by BTK","evidences":[{"source":"PubMed","id":"34554188","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"28943315","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by LATS1 and LATS2","evidences":[{"source":"PubMed","id":"39173637","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8R4B8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine; by CSNK1A1","evidences":[{"source":"PubMed","id":"34615873","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"27043286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues3
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"36586411","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"39173637","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"37575012","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"34615873","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"26037928","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16179258","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31246429","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11337501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20685959","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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