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7X79

The crystal structure of human Calpain-1 protease core in complex with 14b

Functional Information from GO Data
ChainGOidnamespacecontents
A0001533cellular_componentcornified envelope
A0004198molecular_functioncalcium-dependent cysteine-type endopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0008284biological_processpositive regulation of cell population proliferation
A0016020cellular_componentmembrane
A0016241biological_processregulation of macroautophagy
A0032801biological_processreceptor catabolic process
A0046872molecular_functionmetal ion binding
A0050790biological_processregulation of catalytic activity
A0060056biological_processmammary gland involution
A0070062cellular_componentextracellular exosome
A0097264biological_processself proteolysis
A0098989biological_processNMDA selective glutamate receptor signaling pathway
A0110158cellular_componentcalpain complex
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DRDGNGKLGlvEF
ChainResidueDetails
AASP598-PHE610
AASP628-MET640

site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGaLGDCWLlAA
ChainResidueDetails
AGLN109-ALA120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS115
AHIS272
AASN296

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLN109
AASP114
AASN316
AASP318
AASP323

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP598
AGLU639
AASP600
AASN602
ALYS604
AGLU609
AASP628
AASP630
ASER632
ASER634

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; for 78 kDa form
ChainResidueDetails
ASER15

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; for 75 kDa form
ChainResidueDetails
AGLY27

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR354

223790

PDB entries from 2024-08-14

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