Structure of PDB 1fq5 Chain A

Receptor sequence
>1fq5A (length=329) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLA
CFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQ
DFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEK
RFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEG
IGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTL
DCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGP
LAIVGDAFLRKYYSIYDIGNNAVGLAKAI
3D structure
PDB1fq5 X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity.
ChainA
Resolution2.4 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 0GM A Q13 D32 Q74 Y75 G76 T77 T111 G115 F117 I120 I128 D215 G217 T218 S219 F291 Q14 D33 Q75 Y76 G77 T78 T112 G116 F118 I121 I129 D218 G220 T221 S222 F294 MOAD: Ki=4nM
PDBbind-CN: -logKd/Ki=8.40,Ki=4.0nM
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:1fq5, PDBe:1fq5, PDBj:1fq5
PDBsum1fq5
PubMed11061973
UniProtP07267|CARP_YEAST Saccharopepsin (Gene Name=PEP4)

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