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1U5I

Crystal Structure analysis of rat m-calpain mutant Lys10 Thr

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
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
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0110158cellular_componentcalpain complex
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 PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF
ChainResidueDetails
BASP68-PHE80
BASP98-LEU110
AASP585-PHE597
AASP615-MET627

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => 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
BMET29
BSER32
BTHR34
BILE39
BILE57
BPHE145

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
BTHR72
BALA113
AALA542
AASP545
AGLU547
AGLU552
AASP658
AASN661
BLYS74
BGLY76
BGLU78
BLEU83
BSER102
BTHR104
BGLY106
BASN108

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04632
ChainResidueDetails
BTHR99
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

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PDB entries from 2024-07-24

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