Structure of PDB 1wkr Chain A Binding Site BS01

Receptor Information
>1wkr Chain A (length=340) Species: 5319 (Irpex lacteus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAGSVPATNQLVDYVVNVGVGSPATTYSLLVDTGSSNTWLGADKSYVKTS
TSSATSDKVSVTYGSGSFSGTEYTDTVTLGSLTIPKQSIGVASRDSGFDG
VDGILGVGPVDLTVGTLSPHTSTSIPTVTDNLFSQGTIPTNLLAVSFEPT
TSESSTNGELTFGATDSSKYTGSITYTPITSTSPASAYWGINQSIRYGSS
TSILSSTAGIVDTGTTLTLIASDAFAKYKKATGAVADNNTGLLRLTTAQY
ANLQSLFFTIGGQTFELTANAQIWPRNLNTAIGGSASSVYLIVGDLGSDS
GEGLDFINGLTFLERFYSVYDTTNKRLGLATTSFTTATSN
Ligand information
>1wkr Chain I (length=6) Species: 285516 (Streptomyces argenteolus subsp. toyonakensis) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
VVVLAL
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1wkr Crystal Structure of Aspartic Proteinase from Irpex lacteus in Complex with Inhibitor Pepstatin
Resolution1.3 Å
Binding residue
(original residue number in PDB)
L30 D32 G34 Y63 G64 S65 F98 Y188 D212 G214 T215 T216
Binding residue
(residue number reindexed from 1)
L30 D32 G34 Y63 G64 S65 F98 Y188 D212 G214 T215 T216
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.
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1wkr, PDBe:1wkr, PDBj:1wkr
PDBsum1wkr
PubMed15321718
UniProtP17576|CARP_IRPLA Polyporopepsin

[Back to BioLiP]