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1G0V

THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT, MVV

Functional Information from GO Data
ChainGOidnamespacecontents
A0000324cellular_componentfungal-type vacuole
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004866molecular_functionendopeptidase inhibitor activity
B0010951biological_processnegative regulation of endopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VILDTGSSNLWV
ChainResidueDetails
AVAL29-VAL40
AALA212-LEU223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.1
ChainResidueDetails
BMET1
ATHR216

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AGLY68
APHE267

218853

PDB entries from 2024-04-24

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