Structure of PDB 1apv Chain E

Receptor sequence
>1apvE (length=323) Species: 5079 (Penicillium janthinellum) [Search protein sequence]
AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQ
QSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQ
AVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQ
PLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTA
GSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCS
TNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGD
IFLKSQYVVFDSDGPQLGFAPQA
3D structure
PDB1apv Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
ChainE
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.23.20: penicillopepsin.
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 E E15 D33 G35 Y75 G76 D77 D213 G215 T216 T217 E15 D33 G35 Y75 G76 D77 D213 G215 T216 T217
BS02 MAN E S3 G35 S3 G35
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1apv, PDBe:1apv, PDBj:1apv
PDBsum1apv
PubMed1567842
UniProtP00798|PEPA1_PENJA Penicillopepsin-1

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