Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ARY

Catalytic domain of Human Calpain-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004198molecular_functioncalcium-dependent cysteine-type endopeptidase activity
A0006508biological_processproteolysis
B0004198molecular_functioncalcium-dependent cysteine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AVAL99
AGLY101
AASP106
AGLU185
AHOH403
AHOH406

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AASP331
AGLU333
AHOH414
AGLU302
AASP309
AMET329

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BVAL99
BGLY101
BASP106
BGLU185
BHOH442

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BGLU302
BASP309
BMET329
BASP331
BGLU333
BHOH420

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 400
ChainResidue
ATRP116
ALEU247
AGLY249
AGLU349
ACYS351

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 400
ChainResidue
AGLN287
BGLN109
BGLY113
BCYS115
BHIS272

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME B 401
ChainResidue
BTRP116
BLEU247
BGLY249
BGLU349
BCYS351
BHOH503

Functional Information from PROSITE/UniProt
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 Residues598
DetailsDomain: {"description":"Calpain catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00239","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
AHIS272
AGLN109
AASN296
ACYS115

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
BHIS272
BGLN109
BASN296
BCYS115

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
AHIS272
AGLN109
ATRP298
AASN296
ACYS115

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
BHIS272
BGLN109
BTRP298
BASN296
BCYS115

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon