Structure of PDB 3fv3 Chain E

Receptor sequence
>3fv3E (length=339) Species: 5480 (Candida parapsilosis) [Search protein sequence]
DSISLSLINEGPSYASKVSVGSNKQQQTVIIDTGSSDFWVVDSNAQCGKG
VDCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSI
TGQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQ
GKIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQALTIS
LASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARD
QYLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSD
DTILGDNFLRHAYLLYNLDANTISIAQVKYTTDSSISAV
3D structure
PDB3fv3 The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A
ChainE
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 E D32 G34 Y78 G79 D80 D220 G222 T223 T224 Y227 Y285 D32 G34 Y78 G79 D80 D220 G222 T223 T224 Y227 Y285
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3fv3, PDBe:3fv3, PDBj:3fv3
PDBsum3fv3
PubMed19401235
UniProtP32951|CARP1_CANPA Candidapepsin-1 (Gene Name=SAPP1)

[Back to BioLiP]