Structure of PDB 3s0n Chain A Binding Site BS02

Receptor Information
>3s0n Chain A (length=226) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRS
ITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKAS
LTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMD
PQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGAAQGIVSYGR
SDAKPPAVFTRISHYQPWINQILQAN
Ligand information
Ligand ID0BB
InChIInChI=1S/C21H20N2O3S/c1-14-6-4-9-18-20(14)15(13-27-18)12-23-17-8-3-2-7-16(17)22(21(23)26)11-5-10-19(24)25/h2-4,6-9,13H,5,10-12H2,1H3,(H,24,25)
InChIKeyWYBNXPWKJQJMLG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Cc1cccc2scc(CN3C(=O)N(CCCC(O)=O)c4ccccc34)c12
ACDLabs 12.01O=C(O)CCCN2c1ccccc1N(C2=O)Cc3c4c(cccc4sc3)C
OpenEye OEToolkits 1.7.2Cc1cccc2c1c(cs2)CN3c4ccccc4N(C3=O)CCCC(=O)O
FormulaC21 H20 N2 O3 S
Name4-{3-[(4-methyl-1-benzothiophen-3-yl)methyl]-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl}butanoic acid
ChEMBLCHEMBL1807643
DrugBank
ZINCZINC000072178162
PDB chain3s0n Chain A Residue 230 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3s0n Benzimidazolone as potent chymase inhibitor: Modulation of reactive metabolite formation in the hydrophobic (P(1)) region.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		H45 L86 A177 F178 K179 S182 S197 Y198 G199 R200
Binding residue
(residue number reindexed from 1)		H45 L86 A177 F178 K179 S182 S197 Y198 G199 R200
Annotation score1
Binding affinityMOAD: ic50=180nM
PDBbind-CN: -logKd/Ki=6.74,IC50=180nM
BindingDB: IC50=180nM
Enzymatic activity
Catalytic site (original residue number in PDB) H45 D89 K179 G180 D181 S182 G183
Catalytic site (residue number reindexed from 1) H45 D89 K179 G180 D181 S182 G183
Enzyme Commision number 3.4.21.39: chymase.
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0042277 peptide binding
Biological Process
GO:0002003 angiotensin maturation
GO:0006508 proteolysis
GO:0006518 peptide metabolic process
GO:0016485 protein processing
GO:0022617 extracellular matrix disassembly
GO:0030163 protein catabolic process
GO:0030901 midbrain development
GO:0034769 basement membrane disassembly
GO:0045766 positive regulation of angiogenesis
GO:0050727 regulation of inflammatory response
GO:0071333 cellular response to glucose stimulus
GO:0140447 cytokine precursor processing
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0030141 secretory granule
GO:0036464 cytoplasmic ribonucleoprotein granule
GO:0043231 intracellular membrane-bounded organelle
GO:0062023 collagen-containing extracellular matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3s0n, PDBe:3s0n, PDBj:3s0n
PDBsum3s0n
PubMed21733690
UniProtP23946|CMA1_HUMAN Chymase (Gene Name=CMA1)

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