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1QDM

CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005773cellular_componentvacuole
A0006508biological_processproteolysis
A0006629biological_processlipid metabolic process
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0005773cellular_componentvacuole
B0006508biological_processproteolysis
B0006629biological_processlipid metabolic process
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
C0004190molecular_functionaspartic-type endopeptidase activity
C0005773cellular_componentvacuole
C0006508biological_processproteolysis
C0006629biological_processlipid metabolic process
C0008233molecular_functionpeptidase activity
C0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV
ChainResidueDetails
AVAL33-VAL44
AALA220-GLY231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Cleavage"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00415","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR226
AASP223
ASER39
AASP36

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATYR80
AASP223
ASER39
AASP36

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTYR80
BASP223
BSER39
BASP36

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
CTYR80
CASP223
CSER39
CASP36

site_idCSA13
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR226
AASP223
ATHR37
AASP36

site_idCSA14
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTHR226
BASP223
BTHR37
BASP36

site_idCSA15
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
CTHR226
CASP223
CTHR37
CASP36

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP223
AASP36

site_idCSA17
Number of Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP223
BASP36

site_idCSA18
Number of Residues2
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
CASP223
CASP36

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BTHR226
BASP223
BSER39
BASP36

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
CTHR226
CASP223
CSER39
CASP36

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ASER224
AASP223
ATHR37
AASP36

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BSER224
BASP223
BTHR37
BASP36

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
CSER224
CASP223
CTHR37
CASP36

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP223
ASER39
AASP36

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
BASP223
BSER39
BASP36

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
CASP223
CSER39
CASP36

247536

PDB entries from 2026-01-14

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