Structure of PDB 2jt5 Chain A Binding Site BS05

Receptor Information
>2jt5 Chain A (length=161) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYE
GEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWT
KDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQD
DINGIQSLYGP
Ligand information
Ligand IDJT5
InChIInChI=1S/C16H18N2O5S/c19-11-10-18(12-16(20)17-21)24(22,23)15-8-6-14(7-9-15)13-4-2-1-3-5-13/h1-9,19,21H,10-12H2,(H,17,20)
InChIKeyQQDWEVONJRXVDB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OCCN(CC(=O)NO)[S](=O)(=O)c1ccc(cc1)c2ccccc2
OpenEye OEToolkits 1.5.0c1ccc(cc1)c2ccc(cc2)S(=O)(=O)N(CCO)CC(=O)NO
ACDLabs 10.04O=C(NO)CN(CCO)S(=O)(=O)c2ccc(c1ccccc1)cc2
FormulaC16 H18 N2 O5 S
NameN~2~-(biphenyl-4-ylsulfonyl)-N-hydroxy-N~2~-(2-hydroxyethyl)glycinamide
ChEMBLCHEMBL1233772
DrugBankDB08029
ZINCZINC000053683340
PDB chain2jt5 Chain A Residue 1 [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]
PDB2jt5 Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors
ResolutionN/A
Binding residue
(original residue number in PDB)		N162 V163 L164 A165 L197 H201 E202 H205 H211 L218 Y220 P221 L222 Y223
Binding residue
(residue number reindexed from 1)		N75 V76 L77 A78 L110 H114 E115 H118 H124 L131 Y133 P134 L135 Y136
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.74,Ki=18nM
Enzymatic activity
Catalytic site (original residue number in PDB) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H114 E115 H118 H124
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2jt5, PDBe:2jt5, PDBj:2jt5
PDBsum2jt5
PubMed17710450
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]