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6NPY

Cryo-EM structure of NLRP3 bound to NEK7

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0002221biological_processpattern recognition receptor signaling pathway
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
A0006915biological_processapoptotic process
A0006952biological_processdefense response
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007231biological_processosmosensory signaling pathway
A0009595biological_processdetection of biotic stimulus
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
A0032753biological_processpositive regulation of interleukin-4 production
A0035591molecular_functionsignaling adaptor activity
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
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_processpyroptosis
A0070273molecular_functionphosphatidylinositol-4-phosphate binding
A0071222biological_processcellular response to lipopolysaccharide
A0072559cellular_componentNLRP3 inflammasome complex
A0098586biological_processcellular response to virus
A0140297molecular_functionDNA-binding transcription factor binding
A0140299molecular_functionsmall molecule sensor activity
A0140608molecular_functioncysteine-type endopeptidase activator activity
A0140693molecular_functionmolecular condensate scaffold activity
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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
BASP161

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:19941817, ECO:0007744|PDB:2WQN
ChainResidueDetails
BILE40
BLYS63

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Autoinhibitory => ECO:0000269|PubMed:19941817
ChainResidueDetails
BTYR97

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by NEK9 => ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:26522158
ChainResidueDetails
BSER195

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:28943315
ChainResidueDetails
ATYR11

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by BTK => ECO:0000269|PubMed:34554188
ChainResidueDetails
ATYR134
ATYR138
ATYR141
ATYR166

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8R4B8
ChainResidueDetails
ASER159
ASER293

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:28943315
ChainResidueDetails
ASER161
ASER332
ASER726
ASER973

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK8 => ECO:0000269|PubMed:35114687
ChainResidueDetails
ASER196

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:35114687
ChainResidueDetails
ASER199

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphoserine; by CSNK1A1 => ECO:0000269|PubMed:34615873
ChainResidueDetails
ASER733
ASER804
ASER1033

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:27043286
ChainResidueDetails
ATYR859

site_idSWS_FT_FI13
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:36586411
ChainResidueDetails
ACYS842

site_idSWS_FT_FI14
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:26037928
ChainResidueDetails
ALYS687

site_idSWS_FT_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:34615873
ChainResidueDetails
ALYS876
ALYS925
ALYS971

219140

PDB entries from 2024-05-01

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