Structure of PDB 2qzx Chain A

Receptor sequence
>2qzxA (length=342) Species: 5476 (Candida albicans) [Search protein sequence]
GPVAVTLHNEAITYTADITVGSDNQKLNVIVDTGSSDLWIPDSNVICIPK
WRGDKGDFCKSAGSYSPASSRTSQNLNTRFDIKYGDGSYAKGKLYKDTVG
IGGVSVRDQLFANVWSTSARKGILGIGFQSGEATEFDYDNLPISLRNQGI
IGKAAYSLYLNSAEASTGQIIFGGIDKAKYSGSLVDLPITSEKKLTVGLR
SVNVRGRNVDANTNVLLDSGTTISYFTRSIVRNILYAIGAQMKFDSAGNK
VYVADCKTSGTIDFQFGNNLKISVPVSEFLFQTYYTSGKPFPKCEVRIRE
SEDNILGDNFLRSAYVVYNLDDKKISMAPVKYTSESDIVAIN
3D structure
PDB2qzx X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 A D32 G34 K83 Y84 G85 D86 I123 D218 G220 T221 T222 Y225 D32 G34 K83 Y84 G85 D86 I123 D218 G220 T221 T222 Y225
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
PDBsum2qzx
PubMed18384081
UniProtP43094|CARP5_CANAL Secreted aspartic protease 5 (Gene Name=SAP5)

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