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2PRE

Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
AGLY192
AHOH375
BLYS154

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 307
ChainResidue
ACYS63
AVAL92
AGLN93
AHOH370

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 308
ChainResidue
ALYS58
ALYS59
ATYR74
ACYS56
AASN57

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE E64 A 302
ChainResidue
AGLN19
AGLY23
ASER24
ACYS25
ATRP26
AHIS61
ALYS64
AGLY65
AGLY66
AASN156
AHIS157
AHOH356
AHOH357
AHOH367

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
ALYS154
BGLY191
BGLY192
BHOH357

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BCYS56
BASN57
BLYS58
BLYS59
BTYR74

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 306
ChainResidue
AASN44
BLYS101
BGLN182
BHOH356

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE E64 B 301
ChainResidue
BGLN19
BGLY23
BSER24
BCYS25
BTRP26
BHIS61
BLYS64
BGLY65
BGLY66
BASN156
BHIS157
BGLY158

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_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWgryWGeqGYIrM
ChainResidueDetails
ATYR168-MET187

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:2PRE
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

237992

PDB entries from 2025-06-25

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