Structure of PDB 1bxq Chain A Binding Site BS01

Receptor Information
>1bxq Chain A (length=323) Species: 5079 (Penicillium janthinellum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQ
QSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQ
AVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQ
PLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTA
GSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCS
TNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGD
IFLKSQYVVFDSDGPQLGFAPQA
Ligand information
Ligand IDPP8
InChIInChI=1S/C29H47N4O9P/c1-17(2)13-24(35)32-26(19(5)6)28(37)31-21(16-23(30)34)27(36)33-25(14-18(3)4)43(39,40)42-22(29(38)41-7)15-20-11-9-8-10-12-20/h8-12,17-19,21-22,25-26H,13-16H2,1-7H3,(H2,30,34)(H,31,37)(H,32,35)(H,33,36)(H,39,40)/t21-,22-,25+,26-/m0/s1
InChIKeySGKZZKPYLILTJX-RLBRRGQKSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)CC(NC(=O)C(CC(=O)N)NC(=O)C(C(C)C)NC(=O)CC(C)C)P(=O)(O)OC(Cc1ccccc1)C(=O)OC
ACDLabs 10.04O=C(NC(C(=O)NC(C(=O)NC(CC(C)C)P(=O)(OC(C(=O)OC)Cc1ccccc1)O)CC(=O)N)C(C)C)CC(C)C
CACTVS 3.341COC(=O)[CH](Cc1ccccc1)O[P](O)(=O)[CH](CC(C)C)NC(=O)[CH](CC(N)=O)NC(=O)[CH](NC(=O)CC(C)C)C(C)C
OpenEye OEToolkits 1.5.0CC(C)C[C@H](NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C)[P@](=O)(O)O[C@@H](Cc1ccccc1)C(=O)OC
CACTVS 3.341COC(=O)[C@H](Cc1ccccc1)O[P@](O)(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)CC(C)C)C(C)C
FormulaC29 H47 N4 O9 P
Name2-[(1R)-1-(N-(3-METHYLBUTANOYL)-L-VALYL-L-ASPARAGINYL)-AMINO)-3-METHYLBUTYL]HYDROXYPHOSPHINYLOXY]-3-PHENYLPROPANOIC ACID METHYLESTER
ChEMBLCHEMBL557341
DrugBank
ZINCZINC000015297976
PDB chain1bxq Chain A Residue 324 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1bxq Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes.
Resolution1.41 Å
Binding residue
(original residue number in PDB)		E15 D33 Y75 G76 D77 I211 D213 G215 T216 T217 Y274 I293 I297
Binding residue
(residue number reindexed from 1)		E15 D33 Y75 G76 D77 I211 D213 G215 T216 T217 Y274 I293 I297
Annotation score1
Binding affinityMOAD: Ki=42nM
PDBbind-CN: -logKd/Ki=7.38,Ki=42nM
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.
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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