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1KFU

Crystal Structure of Human m-Calpain Form II

Replaces:  1DKV
Functional Information from GO Data
ChainGOidnamespacecontents
L0000785cellular_componentchromatin
L0001666biological_processresponse to hypoxia
L0001824biological_processblastocyst development
L0004198molecular_functioncalcium-dependent cysteine-type endopeptidase activity
L0005509molecular_functioncalcium ion binding
L0005515molecular_functionprotein binding
L0005634cellular_componentnucleus
L0005737cellular_componentcytoplasm
L0005764cellular_componentlysosome
L0005783cellular_componentendoplasmic reticulum
L0005794cellular_componentGolgi apparatus
L0005829cellular_componentcytosol
L0005886cellular_componentplasma membrane
L0005925cellular_componentfocal adhesion
L0006508biological_processproteolysis
L0007520biological_processmyoblast fusion
L0007565biological_processfemale pregnancy
L0008092molecular_functioncytoskeletal protein binding
L0008233molecular_functionpeptidase activity
L0008234molecular_functioncysteine-type peptidase activity
L0009612biological_processresponse to mechanical stimulus
L0009897cellular_componentexternal side of plasma membrane
L0010666biological_processpositive regulation of cardiac muscle cell apoptotic process
L0016540biological_processprotein autoprocessing
L0016787molecular_functionhydrolase activity
L0019899molecular_functionenzyme binding
L0030163biological_processprotein catabolic process
L0030425cellular_componentdendrite
L0030864cellular_componentcortical actin cytoskeleton
L0031143cellular_componentpseudopodium
L0032675biological_processregulation of interleukin-6 production
L0035458biological_processcellular response to interferon-beta
L0042542biological_processresponse to hydrogen peroxide
L0042995cellular_componentcell projection
L0043025cellular_componentneuronal cell body
L0044877molecular_functionprotein-containing complex binding
L0045121cellular_componentmembrane raft
L0046872molecular_functionmetal ion binding
L0048266biological_processbehavioral response to pain
L0048488biological_processsynaptic vesicle endocytosis
L0051493biological_processregulation of cytoskeleton organization
L0051603biological_processproteolysis involved in protein catabolic process
L0070062cellular_componentextracellular exosome
L0071222biological_processcellular response to lipopolysaccharide
L0071230biological_processcellular response to amino acid stimulus
L0097038cellular_componentperinuclear endoplasmic reticulum
L0097225cellular_componentsperm midpiece
L0097228cellular_componentsperm principal piece
L0097700biological_processvascular endothelial cell response to laminar fluid shear stress
L0097706biological_processvascular endothelial cell response to oscillatory fluid shear stress
L0098793cellular_componentpresynapse
L0098794cellular_componentpostsynapse
L0110158cellular_componentcalpain complex
L0120212cellular_componentsperm head-tail coupling apparatus
L0140249biological_processprotein catabolic process at postsynapse
L1901741biological_processpositive regulation of myoblast fusion
L2001247biological_processpositive regulation of phosphatidylcholine biosynthetic process
S0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF
ChainResidueDetails
SASP852-PHE864
SASP882-LEU894
LASP585-PHE597
LASP615-MET627

site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGaLGDCWLlAA
ChainResidueDetails
LGLN99-ALA110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsPropeptide: {"description":"Anchors to the small subunit","featureId":"PRO_0000026487","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues299
DetailsDomain: {"description":"Calpain catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00239","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues33
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues68
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues68
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues169
DetailsRegion: {"description":"Domain III"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues14
DetailsRegion: {"description":"Linker"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues170
DetailsRegion: {"description":"Domain IV"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues15
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues34
DetailsDomain: {"description":"EF-hand 1; atypical","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues28
DetailsDomain: {"description":"EF-hand 4","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues34
DetailsDomain: {"description":"EF-hand 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q64537","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q64537","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 10639123
ChainResidueDetails
LCYS105
LCYS105
LHIS262
LASN286
LGLN99
LTRP288

site_idMCSA1
Number of Residues5
DetailsM-CSA 589
ChainResidueDetails

244349

PDB entries from 2025-11-05

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