Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6N9N

Crystal structure of murine GSDMD

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006954biological_processinflammatory response
A0008289molecular_functionlipid binding
A0009306biological_processprotein secretion
A0012501biological_processprogrammed cell death
A0016020cellular_componentmembrane
A0022829molecular_functionwide pore channel activity
A0031966cellular_componentmitochondrial membrane
A0032731biological_processpositive regulation of interleukin-1 beta production
A0045087biological_processinnate immune response
A0046931biological_processpore complex assembly
A0050729biological_processpositive regulation of inflammatory response
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051260biological_processprotein homooligomerization
A0055085biological_processtransmembrane transport
A0061702cellular_componentcanonical inflammasome complex
A0070269biological_processpyroptotic inflammatory response
A0070273molecular_functionphosphatidylinositol-4-phosphate binding
A0070300molecular_functionphosphatidic acid binding
A0072559cellular_componentNLRP3 inflammasome complex
A0141201biological_processpyroptotic cell death
A1901612molecular_functioncardiolipin binding
B0001786molecular_functionphosphatidylserine binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006954biological_processinflammatory response
B0008289molecular_functionlipid binding
B0009306biological_processprotein secretion
B0012501biological_processprogrammed cell death
B0016020cellular_componentmembrane
B0022829molecular_functionwide pore channel activity
B0031966cellular_componentmitochondrial membrane
B0032731biological_processpositive regulation of interleukin-1 beta production
B0045087biological_processinnate immune response
B0046931biological_processpore complex assembly
B0050729biological_processpositive regulation of inflammatory response
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0051260biological_processprotein homooligomerization
B0055085biological_processtransmembrane transport
B0061702cellular_componentcanonical inflammasome complex
B0070269biological_processpyroptotic inflammatory response
B0070273molecular_functionphosphatidylinositol-4-phosphate binding
B0070300molecular_functionphosphatidic acid binding
B0072559cellular_componentNLRP3 inflammasome complex
B0141201biological_processpyroptotic cell death
B1901612molecular_functioncardiolipin binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTRANSMEM: Beta stranded => ECO:0000250|UniProtKB:P57764
ChainResidueDetails
AGLN92-SER98
ALYS104-ALA109
AGLY181-LEU187
ACYS192-LYS198
BGLN92-SER98
BLYS104-ALA109
BGLY181-LEU187
BCYS192-LYS198

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by CASP3 or CASP7 => ECO:0000269|PubMed:37327784
ChainResidueDetails
AASP88
BASP88

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by caspases CASP1, CASP4/CASP11 and CASP8 => ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:32553275, ECO:0000269|PubMed:38538834, ECO:0000305|PubMed:30135078
ChainResidueDetails
AASP276
BASP276

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Cleavage; by papain => ECO:0000269|PubMed:35794369
ChainResidueDetails
ALEU310
BLEU310

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P57764
ChainResidueDetails
ATYR38
BTYR38

site_idSWS_FT_FI6
Number of Residues18
DetailsMOD_RES: S-(2-succinyl)cysteine => ECO:0000269|PubMed:32820063
ChainResidueDetails
ACYS39
BCYS39
BCYS57
BCYS77
BCYS122
BCYS192
BCYS265
BCYS299
BCYS434
BCYS487
ACYS57
ACYS77
ACYS122
ACYS192
ACYS265
ACYS299
ACYS434
ACYS487

site_idSWS_FT_FI7
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38538834, ECO:0000269|PubMed:38599239
ChainResidueDetails
ACYS192
BCYS192

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon