Structure of PDB 1g0v Chain A

Receptor sequence
>1g0vA (length=329) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLA
CFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQ
DFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEK
RFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEG
IGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGSTGQYTL
DCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGP
LAIVGDAFLRKYYSIYDLGNNAVGLAKAI
3D structure
PDB1g0v The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae.
ChainA
Resolution2.0 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 D32 Y75 T77 T111 I128 R186 A188 Y189 T218 L220 Q244 V278 S279 S281 F291 V295 Y10 L11 D33 Y76 T78 T112 I129 R190 A192 Y193 T221 L223 Q247 V281 S282 S284 F294 V298
BS02 MAN A V134 Y138 V135 Y139
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:1g0v, PDBe:1g0v, PDBj:1g0v
PDBsum1g0v
PubMed11042188
UniProtP07267|CARP_YEAST Saccharopepsin (Gene Name=PEP4)

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