Structure of PDB 3tsk Chain A Binding Site BS06

Receptor Information
>3tsk Chain A (length=159) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG
Ligand information
Ligand IDQEG
InChIInChI=1S/C29H32N4O6S/c30-25(34)13-11-23(29(39)33-22(28(31)38)12-15-27(36)37)32-26(35)14-8-18-6-9-20(10-7-18)24-16-21(17-40-24)19-4-2-1-3-5-19/h1-7,9-10,16-17,22-23H,8,11-15H2,(H2,30,34)(H2,31,38)(H,32,35)(H,33,39)(H,36,37)/t22-,23-/m0/s1
InChIKeyKGPPRBTYRFIDAL-GOTSBHOMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.2c1ccc(cc1)c2cc(sc2)c3ccc(cc3)CCC(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N
OpenEye OEToolkits 1.7.2c1ccc(cc1)c2cc(sc2)c3ccc(cc3)CCC(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)O)C(=O)N
CACTVS 3.370NC(=O)CC[C@H](NC(=O)CCc1ccc(cc1)c2scc(c2)c3ccccc3)C(=O)N[C@@H](CCC(O)=O)C(N)=O
CACTVS 3.370NC(=O)CC[CH](NC(=O)CCc1ccc(cc1)c2scc(c2)c3ccccc3)C(=O)N[CH](CCC(O)=O)C(N)=O
ACDLabs 12.01O=C(O)CCC(C(=O)N)NC(=O)C(NC(=O)CCc3ccc(c2scc(c1ccccc1)c2)cc3)CCC(=O)N
FormulaC29 H32 N4 O6 S
NameN~2~-{3-[4-(4-phenylthiophen-2-yl)phenyl]propanoyl}-L-glutaminyl-L-alpha-glutamine
ChEMBLCHEMBL3675596
DrugBank
ZINCZINC000098209333
PDB chain3tsk Chain A Residue 306 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3tsk Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G179 I180 H218 K233 P238 T239 Y240 K241 V243
Binding residue
(residue number reindexed from 1)		G75 I76 H114 K129 P134 T135 Y136 K137 V139
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.17,Kd=67nM
BindingDB: Ki=317nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H114 E115 H118 H124
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3tsk, PDBe:3tsk, PDBj:3tsk
PDBsum3tsk
PubMed22689580
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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