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3BOW

Structure of M-calpain in complex with Calpastatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0001666biological_processresponse to hypoxia
A0001824biological_processblastocyst development
A0004198molecular_functioncalcium-dependent cysteine-type endopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006508biological_processproteolysis
A0007520biological_processmyoblast fusion
A0007565biological_processfemale pregnancy
A0008092molecular_functioncytoskeletal protein binding
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009612biological_processresponse to mechanical stimulus
A0009897cellular_componentexternal side of plasma membrane
A0010666biological_processpositive regulation of cardiac muscle cell apoptotic process
A0016540biological_processprotein autoprocessing
A0016787molecular_functionhydrolase activity
A0019899molecular_functionenzyme binding
A0030163biological_processprotein catabolic process
A0030425cellular_componentdendrite
A0031143cellular_componentpseudopodium
A0032675biological_processregulation of interleukin-6 production
A0035458biological_processcellular response to interferon-beta
A0042542biological_processresponse to hydrogen peroxide
A0042995cellular_componentcell projection
A0043025cellular_componentneuronal cell body
A0044877molecular_functionprotein-containing complex binding
A0045121cellular_componentmembrane raft
A0046872molecular_functionmetal ion binding
A0048266biological_processbehavioral response to pain
A0048488biological_processsynaptic vesicle endocytosis
A0051603biological_processproteolysis involved in protein catabolic process
A0071222biological_processcellular response to lipopolysaccharide
A0071230biological_processcellular response to amino acid stimulus
A0097038cellular_componentperinuclear endoplasmic reticulum
A0097225cellular_componentsperm midpiece
A0097228cellular_componentsperm principal piece
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0110158cellular_componentcalpain complex
A0120212cellular_componentsperm head-tail coupling apparatus
A0140249biological_processprotein catabolic process at postsynapse
A1901741biological_processpositive regulation of myoblast fusion
A2001247biological_processpositive regulation of phosphatidylcholine biosynthetic process
B0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 715
ChainResidue
AILE89
AGLY91
AASP96
AGLU175
AHOH742
AHOH753

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 716
ChainResidue
AASP321
AGLU323
AHOH835
AGLU292
AASP299
AGLN319

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 717
ChainResidue
AALA542
AASP545
AGLU547
AGLU552
AHOH741

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 718
ChainResidue
AASP585
AASP587
ASER589
ALYS591
AGLU596

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 719
ChainResidue
AASP615
AASP617
ASER619
ATHR621
AGLU626

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 720
ChainResidue
AASP658
AASN661

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BHOH1
BALA111
BASP114
BGLU116
BGLU121
BHOH408

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BASP154
BASP156
BTHR158
BLYS160
BGLU165
BHOH417

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BASP184
BASP186
BSER188
BTHR190
BGLU195

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BASP139
BASP227
BASP229
BASN230

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF
ChainResidueDetails
BASP154-PHE166
BASP184-LEU196
AASP585-PHE597
AASP615-MET627

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues299
DetailsDomain: {"description":"Calpain catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00239","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues68
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues68
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsRegion: {"description":"Linker"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues170
DetailsRegion: {"description":"Domain IV"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PubMed","id":"7635186","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues34
DetailsDomain: {"description":"EF-hand 1; atypical","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues28
DetailsDomain: {"description":"EF-hand 4","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues34
DetailsDomain: {"description":"EF-hand 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19020622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19020623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9228945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DVI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DF0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19020622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19020623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9228945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DVI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DF0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04632","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
AASN286
AHIS262
AGLN99
ASER105

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
AASN286
AHIS262
AGLN99
ASER105
ATRP288

246031

PDB entries from 2025-12-10

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