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3V6L

Crystal Structure of caspase-6 inactivation mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0002218biological_processactivation of innate immune response
A0004175molecular_functionendopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016540biological_processprotein autoprocessing
A0016787molecular_functionhydrolase activity
A0030855biological_processepithelial cell differentiation
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0043067biological_processregulation of programmed cell death
A0043525biological_processpositive regulation of neuron apoptotic process
A0051604biological_processprotein maturation
A0060545biological_processpositive regulation of necroptotic process
A0070269biological_processpyroptotic inflammatory response
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
A0072734biological_processcellular response to staurosporine
A0097284biological_processhepatocyte apoptotic process
B0002218biological_processactivation of innate immune response
B0004175molecular_functionendopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0016540biological_processprotein autoprocessing
B0016787molecular_functionhydrolase activity
B0030855biological_processepithelial cell differentiation
B0042802molecular_functionidentical protein binding
B0043065biological_processpositive regulation of apoptotic process
B0043067biological_processregulation of programmed cell death
B0043525biological_processpositive regulation of neuron apoptotic process
B0051604biological_processprotein maturation
B0060545biological_processpositive regulation of necroptotic process
B0070269biological_processpyroptotic inflammatory response
B0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
B0072734biological_processcellular response to staurosporine
B0097284biological_processhepatocyte apoptotic process
Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HadadCfvCvFLSHG
ChainResidueDetails
AHIS108-GLY122

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKIFIIQACRG
ChainResidueDetails
ALYS154-GLY165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsRegion: {"description":"Tri-arginine exosite","evidences":[{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues34
DetailsRegion: {"description":"130's region","evidences":[{"source":"PubMed","id":"28154009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"16123779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19133298","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19694615","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20890311","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28864531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30420425","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O08738","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by NUAK1 and AMPK","evidences":[{"source":"PubMed","id":"15273717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22483120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32029622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27911442","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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