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2NQA

Catalytic Domain of Human Calpain 8

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 Residues5
DetailsBINDING SITE FOR RESIDUE CA A 901
ChainResidue
AGLU292
AASP299
AVAL319
AASP321
AGLU323

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 902
ChainResidue
BGLU323
BGLU292
BASP299
BVAL319
BASP321

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 903
ChainResidue
AVAL89
AGLY91
AASP96
AGLU175
AHOH1060

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 904
ChainResidue
BVAL89
BGLY91
BASP96
BGLU175
BHOH996

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 905
ChainResidue
AGLU292
AGLU320
BARG311
BGLU314

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR CHAIN D OF LEUPEPTIN INHIBITOR
ChainResidue
AGLY103
ACYS105
AGLY197
AALA250
AGLU251
ASER261
AHIS262
AALA263
BTYR27
BLEU28
BLEU188
BASN189
BGLY190
DHOH98

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR CHAIN E OF LEUPEPTIN INHIBITOR
ChainResidue
ATYR27
ALEU188
AGLY190
BGLY103
BCYS105
BGLY197
BSER261
BHIS262
BHOH1032
EHOH97

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGgLGDCWLlAA
ChainResidueDetails
AGLN99-ALA110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS105
AHIS262
AASN286
BCYS105
BHIS262
BASN286

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL89
AGLY91
AASP96
AGLU175
AARG229
ALYS230
AGLU292
AASP299
AGLU323

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
AASN286
AHIS262
AGLN99
ACYS105

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
BASN286
BHIS262
BGLN99
BCYS105

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
AASN286
AHIS262
AGLN99
ACYS105
ATRP288

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1kfu
ChainResidueDetails
BASN286
BHIS262
BGLN99
BCYS105
BTRP288

site_idMCSA1
Number of Residues5
DetailsM-CSA 589
ChainResidueDetails
AGLN99electrostatic stabiliser
ACYS105electrostatic stabiliser
AHIS262proton acceptor, proton donor
AASN286electrostatic stabiliser
ATRP288steric role

224201

PDB entries from 2024-08-28

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