Structure of PDB 1wkr Chain A

Receptor sequence
>1wkrA (length=340) Species: 5319 (Irpex lacteus) [Search protein sequence]
AAGSVPATNQLVDYVVNVGVGSPATTYSLLVDTGSSNTWLGADKSYVKTS
TSSATSDKVSVTYGSGSFSGTEYTDTVTLGSLTIPKQSIGVASRDSGFDG
VDGILGVGPVDLTVGTLSPHTSTSIPTVTDNLFSQGTIPTNLLAVSFEPT
TSESSTNGELTFGATDSSKYTGSITYTPITSTSPASAYWGINQSIRYGSS
TSILSSTAGIVDTGTTLTLIASDAFAKYKKATGAVADNNTGLLRLTTAQY
ANLQSLFFTIGGQTFELTANAQIWPRNLNTAIGGSASSVYLIVGDLGSDS
GEGLDFINGLTFLERFYSVYDTTNKRLGLATTSFTTATSN
3D structure
PDB1wkr Crystal Structure of Aspartic Proteinase from Irpex lacteus in Complex with Inhibitor Pepstatin
ChainA
Resolution1.3 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 N37 W39 Y63 D212 T215
Catalytic site (residue number reindexed from 1) D32 S35 N37 W39 Y63 D212 T215
Enzyme Commision number 3.4.23.29: polyporopepsin.
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 L30 D32 G34 Y63 G64 S65 F98 Y188 D212 G214 T215 T216 L30 D32 G34 Y63 G64 S65 F98 Y188 D212 G214 T215 T216
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:1wkr, PDBe:1wkr, PDBj:1wkr
PDBsum1wkr
PubMed15321718
UniProtP17576|CARP_IRPLA Polyporopepsin

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