Structure of PDB 2wed Chain A

Receptor sequence
>2wedA (length=323) Species: 5079 (Penicillium janthinellum) [Search protein sequence]
AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQ
QSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQ
AVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQ
PLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTA
GSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCS
TNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGD
IFLKSQYVVFDSDGPQLGFAPQA
3D structure
PDB2wed Crystallographic Analysis of Transition State Mimics Bound to Penicillopepsin: Difluorostatine-and Difluorostatone-Containing Peptides
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D33 S36 D38 W40 Y75 D213 T216
Catalytic site (residue number reindexed from 1) D33 S36 D38 W40 Y75 D213 T216
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 PP6 A D33 G35 Y75 G76 D77 D213 G215 T216 I297 D33 G35 Y75 G76 D77 D213 G215 T216 I297 MOAD: Ki=0.8uM
PDBbind-CN: -logKd/Ki=6.10,Ki=0.8uM
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:2wed, PDBe:2wed, PDBj:2wed
PDBsum2wed
PubMed
UniProtP00798|PEPA1_PENJA Penicillopepsin-1

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