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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4FDL

Crystal structure of Caspase-7

Functional Information from GO Data
ChainGOidnamespacecontents
A0001650cellular_componentfibrillar center
A0001778biological_processplasma membrane repair
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0004190molecular_functionaspartic-type endopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0007507biological_processheart development
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009411biological_processresponse to UV
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0042742biological_processdefense response to bacterium
A0043525biological_processpositive regulation of neuron apoptotic process
A0044346biological_processfibroblast apoptotic process
A0046513biological_processceramide biosynthetic process
A0051146biological_processstriated muscle cell differentiation
A0051402biological_processneuron apoptotic process
A0051604biological_processprotein maturation
A0070227biological_processlymphocyte apoptotic process
A0071222biological_processcellular response to lipopolysaccharide
A0071887biological_processleukocyte apoptotic process
A0072734biological_processcellular response to staurosporine
A0097194biological_processexecution phase of apoptosis
A1905686biological_processpositive regulation of plasma membrane repair
B0001650cellular_componentfibrillar center
B0001778biological_processplasma membrane repair
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0007507biological_processheart development
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0009411biological_processresponse to UV
B0016485biological_processprotein processing
B0016787molecular_functionhydrolase activity
B0030163biological_processprotein catabolic process
B0042742biological_processdefense response to bacterium
B0043525biological_processpositive regulation of neuron apoptotic process
B0044346biological_processfibroblast apoptotic process
B0046513biological_processceramide biosynthetic process
B0051146biological_processstriated muscle cell differentiation
B0051402biological_processneuron apoptotic process
B0051604biological_processprotein maturation
B0070227biological_processlymphocyte apoptotic process
B0071222biological_processcellular response to lipopolysaccharide
B0071887biological_processleukocyte apoptotic process
B0072734biological_processcellular response to staurosporine
B0097194biological_processexecution phase of apoptosis
B1905686biological_processpositive regulation of plasma membrane repair
Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HtnaaCfaCiLLSHG
ChainResidueDetails
AHIS131-GLY145
site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKLFFIQACRG
ChainResidueDetails
ALYS177-GLY188
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsRegion: {"description":"Loop L1","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues18
DetailsRegion: {"description":"Loop L2","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsRegion: {"description":"Loop L3","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues28
DetailsRegion: {"description":"Loop L4","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11701129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16916640","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Involved in allosteric regulation","evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581639","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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