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3DF0

Calcium-dependent complex between m-calpain and 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
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
A0051603biological_processproteolysis involved in protein catabolic process
A0071222biological_processcellular response to lipopolysaccharide
A0071230biological_processcellular response to amino acid stimulus
A0097038cellular_componentperinuclear endoplasmic reticulum
A0110158cellular_componentcalpain complex
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 Residues5
DetailsBINDING SITE FOR RESIDUE CA A 715
ChainResidue
AILE89
AGLY90
AGLY91
AASP96
AGLU175

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 716
ChainResidue
AGLU323
AGLU292
AASP299
AGLN319
AASP321

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 717
ChainResidue
AALA542
AASP545
AALA546
AGLU547
AGLU552

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 718
ChainResidue
AGLU547
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 Residues4
DetailsBINDING SITE FOR RESIDUE CA A 720
ChainResidue
AASP570
AASP658
AASP660
AASN661

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 601
ChainResidue
BALA111
BASP114
BGLU116
BGLU121

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA B 602
ChainResidue
BGLU116
BASP154
BASP156
BTHR158
BLYS160
BLEU161
BGLY162
BGLU165

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 603
ChainResidue
BASP184
BASP186
BSER188
BTHR190
BGLU195

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 604
ChainResidue
BASP139
BASP227
BASP229
BASN230

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
CSER203
BASP114
BGLU116
BGLU121
BASP139
BASP227

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0
ChainResidueDetails
BASP154
BGLU195
AALA542
AASP545
AGLU547
AGLU552
AASP658
AASN661
BASP156
BTHR158
BLYS160
BGLU165
BASP184
BASP186
BSER188
BTHR190

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04632
ChainResidueDetails
BLYS181
AGLU626
AASP587
ASER589
ALYS591
AGLU596
AASP615
AASP617
ASER619
ATHR621

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P17655
ChainResidueDetails
AALA2

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

219140

PDB entries from 2024-05-01

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