Structure of PDB 6eox Chain A Binding Site BS06

Receptor Information
>6eox Chain A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG
Ligand information
Ligand IDBKW
InChIInChI=1S/C21H18O5S/c1-26-18-10-6-15(7-11-18)16-8-12-19(13-9-16)27(24,25)20-5-3-2-4-17(20)14-21(22)23/h2-13H,14H2,1H3,(H,22,23)
InChIKeyFIPYOKGRSDJCAR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385COc1ccc(cc1)c2ccc(cc2)[S](=O)(=O)c3ccccc3CC(O)=O
OpenEye OEToolkits 2.0.6COc1ccc(cc1)c2ccc(cc2)S(=O)(=O)c3ccccc3CC(=O)O
FormulaC21 H18 O5 S
Name2-[2-[4-(4-methoxyphenyl)phenyl]sulfonylphenyl]ethanoic acid
ChEMBLCHEMBL573936
DrugBank
ZINCZINC000045285873
PDB chain6eox Chain A Residue 306 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6eox Development of Thioaryl-Based Matrix Metalloproteinase-12 Inhibitors with Alternative Zinc-Binding Groups: Synthesis, Potentiometric, NMR, and Crystallographic Studies.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		I180 L181 A182 H218 E219 H222 H228 V235 F237 P238 T239 Y240
Binding residue
(residue number reindexed from 1)		I75 L76 A77 H113 E114 H117 H123 V130 F132 P133 T134 Y135
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=6.85,IC50=140nM
BindingDB: IC50=140nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
Enzyme Commision number 3.4.24.65: macrophage elastase.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6eox, PDBe:6eox, PDBj:6eox
PDBsum6eox
PubMed29727184
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

[Back to BioLiP]