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

3NR2

Crystal structure of Caspase-6 zymogen

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
A0008234molecular_functioncysteine-type peptidase activity
A0016540biological_processprotein autoprocessing
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
A0097153molecular_functioncysteine-type endopeptidase activity involved in apoptotic process
A0097194biological_processexecution phase of apoptosis
A0097200molecular_functioncysteine-type endopeptidase activity involved in execution phase of apoptosis
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
B0008234molecular_functioncysteine-type peptidase activity
B0016540biological_processprotein autoprocessing
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
B0097153molecular_functioncysteine-type endopeptidase activity involved in apoptotic process
B0097194biological_processexecution phase of apoptosis
B0097200molecular_functioncysteine-type endopeptidase activity involved in execution phase of apoptosis
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:30420425
ChainResidueDetails
AHIS121
BHIS121

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:16123779, ECO:0000269|PubMed:19133298, ECO:0000269|PubMed:19694615, ECO:0000269|PubMed:20890311, ECO:0000269|PubMed:28864531, ECO:0000269|PubMed:30420425
ChainResidueDetails
AALA163
BALA163

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08738
ChainResidueDetails
ASER79
BSER79

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by NUAK1 and AMPK => ECO:0000269|PubMed:15273717, ECO:0000269|PubMed:22483120, ECO:0000269|PubMed:32029622
ChainResidueDetails
ASER257
BSER257

site_idSWS_FT_FI5
Number of Residues4
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27911442
ChainResidueDetails
ACYS264
ACYS277
BCYS264
BCYS277

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon