Structure of PDB 4ryg Chain B Binding Site BS01

Receptor Information
>4ryg Chain B (length=337) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSK
CSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVG
GITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQ
GVLKEDVFSFYYNRDSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQI
QMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLF
DYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAM
DIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
Ligand information
Ligand ID3ZJ
InChIInChI=1S/C27H39N3O6S/c1-20(2)30(27(31)22-11-12-25(35-4)26(15-22)36-14-8-13-34-3)18-23-16-28-17-24(23)29-37(32,33)19-21-9-6-5-7-10-21/h5-7,9-12,15,20,23-24,28-29H,8,13-14,16-19H2,1-4H3/t23-,24+/m0/s1
InChIKeyWPSURGXSNWIBBJ-BJKOFHAPSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=S(=O)(NC2C(CN(C(=O)c1ccc(OC)c(OCCCOC)c1)C(C)C)CNC2)Cc3ccccc3
OpenEye OEToolkits 1.7.6CC(C)N(CC1CNCC1NS(=O)(=O)Cc2ccccc2)C(=O)c3ccc(c(c3)OCCCOC)OC
CACTVS 3.385COCCCOc1cc(ccc1OC)C(=O)N(C[CH]2CNC[CH]2N[S](=O)(=O)Cc3ccccc3)C(C)C
CACTVS 3.385COCCCOc1cc(ccc1OC)C(=O)N(C[C@@H]2CNC[C@H]2N[S](=O)(=O)Cc3ccccc3)C(C)C
OpenEye OEToolkits 1.7.6CC(C)N(C[C@@H]1CNC[C@H]1NS(=O)(=O)Cc2ccccc2)C(=O)c3ccc(c(c3)OCCCOC)OC
FormulaC27 H39 N3 O6 S
NameN-({(3S,4S)-4-[(benzylsulfonyl)amino]pyrrolidin-3-yl}methyl)-4-methoxy-3-(3-methoxypropoxy)-N-(propan-2-yl)benzamide
ChEMBLCHEMBL3401541
DrugBank
ZINCZINC000143600531
PDB chain4ryg Chain B Residue 1001 [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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PDB4ryg trans-(3S,4S)-Disubstituted pyrrolidines as inhibitors of the human aspartyl protease renin. Part I: Prime site exploration using an amino linker.
Resolution2.65 Å
Binding residue
(original residue number in PDB)		T12 Q13 Y14 V30 D32 G34 Y75 S76 T77 P111 L114 F117 L213 D215 G217 A218 I291 T295
Binding residue
(residue number reindexed from 1)		T18 Q19 Y20 V36 D38 G40 Y83 S84 T85 P118 L121 F124 L221 D223 G225 A226 I302 T306
Annotation score1
Binding affinityBindingDB: IC50=8.0nM
Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 W39 Y75 D215 A218
Catalytic site (residue number reindexed from 1) D38 S41 N43 W45 Y83 D223 A226
Enzyme Commision number 3.4.23.15: renin.
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ryg, PDBe:4ryg, PDBj:4ryg
PDBsum4ryg
PubMed25782742
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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