Structure of PDB 1bxq Chain A

Receptor sequence
>1bxqA (length=323) Species: 5079 (Penicillium janthinellum) [Search protein sequence]
AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQ
QSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQ
AVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQ
PLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTA
GSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCS
TNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGD
IFLKSQYVVFDSDGPQLGFAPQA
3D structure
PDB1bxq Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes.
ChainA
Resolution1.41 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 PP8 A E15 D33 Y75 G76 D77 I211 D213 G215 T216 T217 Y274 I293 I297 E15 D33 Y75 G76 D77 I211 D213 G215 T216 T217 Y274 I293 I297 MOAD: Ki=42nM
PDBbind-CN: -logKd/Ki=7.38,Ki=42nM
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:1bxq, PDBe:1bxq, PDBj:1bxq
PDBsum1bxq
PubMed9836576
UniProtP00798|PEPA1_PENJA Penicillopepsin-1

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