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1O0E

1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C

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 Residues5
DetailsBINDING SITE FOR RESIDUE THJ A 601
ChainResidue
AGLY23
ASER24
ACYS25
AHIS157
AHOH708

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE THJ B 601
ChainResidue
BGLY66
BGLY158
BGLY23
BSER24
BCYS25
BTRP26

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

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvRNSWgryWGekGYIrM
ChainResidueDetails
ATYR168-MET187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088
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:0000250|UniProtKB:A8DS38
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

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PDB entries from 2024-07-24

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