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8FVU

Cryo-EM structure of human Needle/NAIP/NLRC4 (R288A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002221biological_processpattern recognition receptor signaling pathway
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006915biological_processapoptotic process
A0006954biological_processinflammatory response
A0007399biological_processnervous system development
A0010804biological_processnegative regulation of tumor necrosis factor-mediated signaling pathway
A0016045biological_processdetection of bacterium
A0016323cellular_componentbasolateral plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0032731biological_processpositive regulation of interleukin-1 beta production
A0042742biological_processdefense response to bacterium
A0042981biological_processregulation of apoptotic process
A0043027molecular_functioncysteine-type endopeptidase inhibitor activity involved in apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0043524biological_processnegative regulation of neuron apoptotic process
A0045087biological_processinnate immune response
A0046330biological_processpositive regulation of JNK cascade
A0046456biological_processicosanoid biosynthetic process
A0046872molecular_functionmetal ion binding
A0050729biological_processpositive regulation of inflammatory response
A0061702cellular_componentcanonical inflammasome complex
A0070269biological_processpyroptotic inflammatory response
A0072557cellular_componentIPAF inflammasome complex
A0120283molecular_functionprotein serine/threonine kinase binding
A2000117biological_processnegative regulation of cysteine-type endopeptidase activity
B0000287molecular_functionmagnesium ion binding
B0002218biological_processactivation of innate immune response
B0002221biological_processpattern recognition receptor signaling pathway
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006915biological_processapoptotic process
B0006954biological_processinflammatory response
B0010954biological_processpositive regulation of protein processing
B0016045biological_processdetection of bacterium
B0032731biological_processpositive regulation of interleukin-1 beta production
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042981biological_processregulation of apoptotic process
B0043065biological_processpositive regulation of apoptotic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0045087biological_processinnate immune response
B0046456biological_processicosanoid biosynthetic process
B0050729biological_processpositive regulation of inflammatory response
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0051260biological_processprotein homooligomerization
B0061133molecular_functionendopeptidase activator activity
B0061702cellular_componentcanonical inflammasome complex
B0070269biological_processpyroptotic inflammatory response
B0072557cellular_componentIPAF inflammasome complex
B0089720molecular_functioncaspase binding
B0097202biological_processactivation of cysteine-type endopeptidase activity
U0003824molecular_functioncatalytic activity
U0005576cellular_componentextracellular region
U0008237molecular_functionmetallopeptidase activity
U0015031biological_processprotein transport
U0030254biological_processprotein secretion by the type III secretion system
U0030257cellular_componenttype III protein secretion system complex
U0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS01282
Number of Residues68
DetailsBIR_REPEAT_1 BIR repeat. EakRlktfvt.Yepysswipqemaa.AGFyFtgvkSgiqCfcCslilfgAgltrlpiedHkrfhPdCgfL
ChainResidueDetails
AGLU60-LEU127
AGLU159-LEU227
AGLU278-LEU345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00136
ChainResidueDetails
BGLY169
ACYS318
AHIS335
ACYS342

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3UP24
ChainResidueDetails
BSER533

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 641
ChainResidueDetails

227344

PDB entries from 2024-11-13

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