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3BCN

Crystal structure of a papain-like cysteine protease Ervatamin-A complexed with irreversible inhibitor E-64

Replaces:  2PSC
Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0051603biological_processproteolysis involved in protein catabolic process
B0004197molecular_functioncysteine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005764cellular_componentlysosome
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
B0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE E64 A 214
ChainResidue
AGLN19
AHIS157
AARG177
AHIS178
AGLN182
BLYS137
AGLY23
ASER24
ACYS25
ATRP26
AGLY65
AGLY66
AALA131
AASN156

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE E64 B 215
ChainResidue
BGLN19
BGLY23
BCYS25
BTRP26
BGLY65
BGLY66
BPHE68
BALA131
BLEU155
BASN156
BHIS157
BGLN182

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 216
ChainResidue
AASP69
AGLN73
ACYS108

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGkCGSCWAfST
ChainResidueDetails
AGLN19-THR30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LNHGVVIVGYG
ChainResidueDetails
ALEU155-GLY165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000305|PubMed:18167146
ChainResidueDetails
ACYS25
BCYS25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089
ChainResidueDetails
AHIS157
BHIS157

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090
ChainResidueDetails
AASN173
BASN173

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:18167146, ECO:0007744|PDB:3BCN
ChainResidueDetails
ACYS25
BCYS25

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
ACYS25
AASN173
AHIS157

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BCYS25
BASN173
BHIS157

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN19
ACYS25
AHIS157

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN19
BCYS25
BHIS157

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN19
AASN173
AHIS157

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN19
BASN173
BHIS157

223790

PDB entries from 2024-08-14

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