Structure of PDB 3tne Chain A

Receptor sequence
>3tneA (length=339) Species: 5480 (Candida parapsilosis) [Search protein sequence]
DSISLSLINEGPSYASKVSVGSNKQQQTVIIDTGSSDFWVVDSNAQCGKG
VDCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSI
TGQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQ
GKIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQALTIS
LASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARD
QYLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSD
DTILGDNFLRHAYLLYNLDANTISIAQVKYTTDSSISAV
3D structure
PDB3tne The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir.
ChainA
Resolution2.4 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 RIT A D32 G34 Y78 G79 D80 S82 V113 N125 D220 G222 T223 T224 Y227 I303 D32 G34 Y78 G79 D80 S82 V113 N125 D220 G222 T223 T224 Y227 I303 PDBbind-CN: -logKd/Ki=5.72,Ki=1.9uM
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:3tne, PDBe:3tne, PDBj:3tne
PDBsum3tne
PubMed22146051
UniProtP32951|CARP1_CANPA Candidapepsin-1 (Gene Name=SAPP1)

[Back to BioLiP]