Structure of PDB 2h6t Chain A

Receptor sequence
>2h6tA (length=340) Species: 5476 (Candida albicans) [Search protein sequence]
QTVPVKLINEQVSYASDITVGSNKQKLTVVIDTGSSDLWVPDSQVSCQAG
QGQDPNFCKNEGTYSPSSSSSSQNLNSPFSIEYGDGTTSQGTWYKDTIGF
GGISITKQQFADVTSTSVDQGILGIGYKTHEAEGNYDNVPVTLKNQGIIS
KNAYSLYLNSRQATSGQIIFGGVDNAKYSGTLIALPVTSDNELRIHLNTV
KVAGQSINADVDVLLDSGTTITYLQQGVADQVISAFNGQETYDANGNLFY
LVDCNLSGSVDFAFDKNAKISVPASEFTAPLYTEDGQVYDQCQLLFGTSD
YNILGDNFLRSAYIVYDLDDNEISLAQVKYTTASNIAALT
3D structure
PDB2h6t The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A.
ChainA
Resolution1.9 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 Y83 D216 T219
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 S35 E83 Y84 G85 D86 D218 G220 T221 T222 Y303 D32 G34 S35 E82 Y83 G84 D85 D216 G218 T219 T220 Y301
BS02 ZN A H197 D214 H196 D212
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:2h6t, PDBe:2h6t, PDBj:2h6t
PDBsum2h6t
PubMed17510964
UniProtP0CY29|CARP3_CANAL Secreted aspartic protease 3 (Gene Name=SAP3)

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