Structure of PDB 1usn Chain A Binding Site BS06

Receptor Information
>1usn Chain A (length=165) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYG
Ligand information
Ligand IDIN9
InChIInChI=1S/C13H10F5N5O2S2/c1-19-10(24)4(20-11(25)21-12-22-23-13(26)27-12)2-3-5(14)7(16)9(18)8(17)6(3)15/h4H,2H2,1H3,(H,19,24)(H,23,26)(H2,20,21,22,25)/t4-/m0/s1
InChIKeyHZAXNPDJVFUGDS-BYPYZUCNSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CNC(=O)[CH](Cc1c(F)c(F)c(F)c(F)c1F)NC(=O)Nc2sc(S)nn2
ACDLabs 10.04O=C(Nc1nnc(S)s1)NC(C(=O)NC)Cc2c(F)c(F)c(F)c(F)c2F
CACTVS 3.341CNC(=O)[C@H](Cc1c(F)c(F)c(F)c(F)c1F)NC(=O)Nc2sc(S)nn2
OpenEye OEToolkits 1.5.0CNC(=O)[C@H](Cc1c(c(c(c(c1F)F)F)F)F)NC(=O)Nc2nnc(s2)S
OpenEye OEToolkits 1.5.0CNC(=O)C(Cc1c(c(c(c(c1F)F)F)F)F)NC(=O)Nc2nnc(s2)S
FormulaC13 H10 F5 N5 O2 S2
Name2-[3-(5-MERCAPTO-[1,3,4]THIADIAZOL-2YL)-UREIDO]-N-METHYL-3-PENTAFLUOROPHENYL-PROPIONAMIDE;
PNU-142372
ChEMBLCHEMBL290140
DrugBankDB07988
ZINCZINC000001545874
PDB chain1usn Chain A Residue 300 [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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PDB1usn Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		Y155 H166 A167 Y168 A169 E202 H205 H211
Binding residue
(residue number reindexed from 1)		Y73 H84 A85 Y86 A87 E120 H123 H129
Annotation score1
Binding affinityMOAD: Ki=0.018uM
PDBbind-CN: -logKd/Ki=7.74,Ki=0.018uM
BindingDB: Ki=18nM
Enzymatic activity
Catalytic site (original residue number in PDB) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
Enzyme Commision number 3.4.24.17: stromelysin 1.
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

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1usn, PDBe:1usn, PDBj:1usn
PDBsum1usn
PubMed9792098
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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