Structure of PDB 1dpj Chain A

Receptor sequence
>1dpjA (length=329) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLA
CFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQ
DFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEK
RFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEG
IGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTL
DCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGP
LAIVGDAFLRKYYSIYDLGNNAVGLAKAI
3D structure
PDB1dpj The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 W39 Y75 D215 T218
Catalytic site (residue number reindexed from 1) D33 S36 N38 W40 Y76 D218 T221
Enzyme Commision number 3.4.23.25: saccharopepsin.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A Y9 L10 Y75 T77 T111 F114 R186 A188 Y189 T218 L220 Q244 S279 S281 M289 F291 V295 Y10 L11 Y76 T78 T112 F115 R190 A192 Y193 T221 L223 Q247 S282 S284 M292 F294 V298
BS02 MAN A K98 V134 K99 V135
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0000324 fungal-type vacuole

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dpj, PDBe:1dpj, PDBj:1dpj
PDBsum1dpj
PubMed10655612
UniProtP07267|CARP_YEAST Saccharopepsin (Gene Name=PEP4)

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