Structure of PDB 2qzx Chain A Binding Site BS01
Receptor Information
>2qzx Chain A (length=342) Species:
5476
(Candida albicans) [
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GPVAVTLHNEAITYTADITVGSDNQKLNVIVDTGSSDLWIPDSNVICIPK
WRGDKGDFCKSAGSYSPASSRTSQNLNTRFDIKYGDGSYAKGKLYKDTVG
IGGVSVRDQLFANVWSTSARKGILGIGFQSGEATEFDYDNLPISLRNQGI
IGKAAYSLYLNSAEASTGQIIFGGIDKAKYSGSLVDLPITSEKKLTVGLR
SVNVRGRNVDANTNVLLDSGTTISYFTRSIVRNILYAIGAQMKFDSAGNK
VYVADCKTSGTIDFQFGNNLKISVPVSEFLFQTYYTSGKPFPKCEVRIRE
SEDNILGDNFLRSAYVVYNLDDKKISMAPVKYTSESDIVAIN
Ligand information
>2qzx Chain C (length=6) Species:
285516
(Streptomyces argenteolus subsp. toyonakensis) [
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VVVLAL
Receptor-Ligand Complex Structure
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PDB
2qzx
X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
D32 G34 K83 Y84 G85 D86 I123 D218 G220 T221 T222 Y225
Binding residue
(residue number reindexed from 1)
D32 G34 K83 Y84 G85 D86 I123 D218 G220 T221 T222 Y225
Enzymatic activity
Catalytic site (original residue number in PDB)
D32 S35 D37 W39 Y84 D218 T221
Catalytic site (residue number reindexed from 1)
D32 S35 D37 W39 Y84 D218 T221
Enzyme Commision number
3.4.23.24
: candidapepsin.
Gene Ontology
Molecular Function
GO:0004190
aspartic-type endopeptidase activity
Biological Process
GO:0006508
proteolysis
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Molecular Function
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Biological Process
External links
PDB
RCSB:2qzx
,
PDBe:2qzx
,
PDBj:2qzx
PDBsum
2qzx
PubMed
18384081
UniProt
P43094
|CARP5_CANAL Secreted aspartic protease 5 (Gene Name=SAP5)
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