Structure of PDB 1dpj Chain A Binding Site BS01
Receptor Information
>1dpj Chain A (length=329) Species:
4932
(Saccharomyces cerevisiae) [
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GGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLA
CFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQ
DFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEK
RFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEG
IGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTL
DCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGP
LAIVGDAFLRKYYSIYDLGNNAVGLAKAI
Ligand information
>1dpj Chain B (length=29) Species:
4932
(Saccharomyces cerevisiae) [
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TDQQKVSEIFQSSKEKLQGDAKVVSDAFK
Receptor-Ligand Complex Structure
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PDB
1dpj
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
Y9 L10 Y75 T77 T111 F114 R186 A188 Y189 T218 L220 Q244 S279 S281 M289 F291 V295
Binding residue
(residue number reindexed from 1)
Y10 L11 Y76 T78 T112 F115 R190 A192 Y193 T221 L223 Q247 S282 S284 M292 F294 V298
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.
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
PDBsum
1dpj
PubMed
10655612
UniProt
P07267
|CARP_YEAST Saccharopepsin (Gene Name=PEP4)
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