Structure of PDB 3fv3 Chain D

Receptor sequence
>3fv3D (length=338) Species: 5480 (Candida parapsilosis) [Search protein sequence]
DSISLSLINEGPSYASKVSVGSNKQQTVIIDTGSSDFWVVDSNAQCGKGV
DCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSIT
GQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQG
KIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQALTISL
ASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARDQ
YLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSDD
TILGDNFLRHAYLLYNLDANTISIAQVKYTTDSSISAV
3D structure
PDB3fv3 The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A
ChainD
Resolution1.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.23.24: candidapepsin.
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 D D32 G34 Y78 G79 D80 D220 G222 T223 T224 Y227 Y285 D301 I303 D31 G33 Y77 G78 D79 D219 G221 T222 T223 Y226 Y284 D300 I302
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
PDBsum3fv3
PubMed19401235
UniProtP32951|CARP1_CANPA Candidapepsin-1 (Gene Name=SAPP1)

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