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1FMU

STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000324cellular_componentfungal-type vacuole
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VILDTGSSNLWV
ChainResidueDetails
AVAL29-VAL40
AALA214-LEU225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP32

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP217

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ASER35
AASP32
ATHR220
AASP217

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR218
AASP32
ATHR33
AASP217

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ASER35
AASP32
AASP217

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATYR75
ASER35
AASP32
AASP217

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP32
ATHR220
ATHR33
AASP217

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PDB entries from 2025-12-24

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