Structure of PDB 2h6t Chain A Binding Site BS01
Receptor Information
>2h6t Chain A (length=340) Species:
5476
(Candida albicans) [
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QTVPVKLINEQVSYASDITVGSNKQKLTVVIDTGSSDLWVPDSQVSCQAG
QGQDPNFCKNEGTYSPSSSSSSQNLNSPFSIEYGDGTTSQGTWYKDTIGF
GGISITKQQFADVTSTSVDQGILGIGYKTHEAEGNYDNVPVTLKNQGIIS
KNAYSLYLNSRQATSGQIIFGGVDNAKYSGTLIALPVTSDNELRIHLNTV
KVAGQSINADVDVLLDSGTTITYLQQGVADQVISAFNGQETYDANGNLFY
LVDCNLSGSVDFAFDKNAKISVPASEFTAPLYTEDGQVYDQCQLLFGTSD
YNILGDNFLRSAYIVYDLDDNEISLAQVKYTTASNIAALT
Ligand information
>2h6t Chain B (length=6) Species:
285516
(Streptomyces argenteolus subsp. toyonakensis) [
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VVVLAL
Receptor-Ligand Complex Structure
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PDB
2h6t
The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
D32 G34 S35 E83 Y84 G85 D86 D218 G220 T221 T222 Y303
Binding residue
(residue number reindexed from 1)
D32 G34 S35 E82 Y83 G84 D85 D216 G218 T219 T220 Y301
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.
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
PDBsum
2h6t
PubMed
17510964
UniProt
P0CY29
|CARP3_CANAL Secreted aspartic protease 3 (Gene Name=SAP3)
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