Structure of PDB 1apt Chain E

Receptor sequence
>1aptE (length=323) Species: 5079 (Penicillium janthinellum) [Search protein sequence]
AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQ
QSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQ
AVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQ
PLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTA
GSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCS
TNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGD
IFLKSQYVVFDSDGPQLGFAPQA
3D structure
PDB1apt Conformational Flexibility in the Active Sites of Aspartyl Proteinases Revealed by a Pepstatin Fragment Binding to Penicillopepsin
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 D33 Y75 G76 D77 D213 G215 T216 T217 D33 Y75 G76 D77 D213 G215 T216 T217
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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Biological Process
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Cellular Component
External links
PDB RCSB:1apt, PDBe:1apt, PDBj:1apt
PDBsum1apt
PubMed
UniProtP00798|PEPA1_PENJA Penicillopepsin-1

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