Structure of PDB 3fv3 Chain A Binding Site BS01
Receptor Information
>3fv3 Chain A (length=339) Species:
5480
(Candida parapsilosis) [
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DSISLSLINEGPSYASKVSVGSNKQQQTVIIDTGSSDFWVVDSNAQCGKG
VDCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSI
TGQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQ
GKIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQALTIS
LASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARD
QYLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSD
DTILGDNFLRHAYLLYNLDANTISIAQVKYTTDSSISAV
Ligand information
>3fv3 Chain I (length=6) Species:
285516
(Streptomyces argenteolus subsp. toyonakensis) [
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VVVLAL
Receptor-Ligand Complex Structure
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PDB
3fv3
The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A
Resolution
1.85 Å
Binding residue
(original residue number in PDB)
D32 G34 Y78 G79 D80 D220 G222 T223 T224 Y227 Y285 D301
Binding residue
(residue number reindexed from 1)
D32 G34 Y78 G79 D80 D220 G222 T223 T224 Y227 Y285 D301
Enzymatic activity
Catalytic site (original residue number in PDB)
D32 S35 D37 W39 Y78 D220 T223
Catalytic site (residue number reindexed from 1)
D32 S35 D37 W39 Y78 D220 T223
Enzyme Commision number
3.4.23.24
: candidapepsin.
Gene Ontology
Molecular Function
GO:0004190
aspartic-type endopeptidase activity
Biological Process
GO:0006508
proteolysis
Cellular Component
GO:0005576
extracellular region
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3fv3
,
PDBe:3fv3
,
PDBj:3fv3
PDBsum
3fv3
PubMed
19401235
UniProt
P32951
|CARP1_CANPA Candidapepsin-1 (Gene Name=SAPP1)
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