Structure of PDB 2hu6 Chain A Binding Site BS06

Receptor Information
>2hu6 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 ID37A
InChIInChI=1S/C20H21N3O5/c24-19(18-16-11-23(20(25)22-26)12-17(27-16)28-18)21-10-13-6-8-15(9-7-13)14-4-2-1-3-5-14/h1-9,16-18,26H,10-12H2,(H,21,24)(H,22,25)/t16-,17-,18+/m0/s1
InChIKeyPPLDARNGJSQINK-OKZBNKHCSA-N
SMILES
SoftwareSMILES
CACTVS 3.341ONC(=O)N1C[C@H]2O[C@@H](C1)[C@@H](O2)C(=O)NCc3ccc(cc3)c4ccccc4
CACTVS 3.341ONC(=O)N1C[CH]2O[CH](C1)[CH](O2)C(=O)NCc3ccc(cc3)c4ccccc4
ACDLabs 10.04O=C(N4CC3OC(C(=O)NCc2ccc(c1ccccc1)cc2)C(O3)C4)NO
OpenEye OEToolkits 1.5.0c1ccc(cc1)c2ccc(cc2)CNC(=O)C3C4CN(CC(O4)O3)C(=O)NO
OpenEye OEToolkits 1.5.0c1ccc(cc1)c2ccc(cc2)CNC(=O)[C@H]3[C@@H]4CN(C[C@@H](O4)O3)C(=O)NO
FormulaC20 H21 N3 O5
Name(1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDE;
(1S,5S,7R)-3-AZA-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-3,7-DICARBOXYLIC ACID 7-[(BIPHENYL-4-YLMETHYL)-AMIDE]-3-HYDROXYAMIDE
ChEMBL
DrugBankDB07026
ZINCZINC000053683784
PDB chain2hu6 Chain A Residue 400 [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]
PDB2hu6 Synthesis of bicyclic molecular scaffolds (BTAa): an investigation towards new selective MMP-12 inhibitors.
Resolution1.32 Å
Binding residue
(original residue number in PDB)		G179 I180 L181 H218 V235 F237 P238 T239 Y240 K241
Binding residue
(residue number reindexed from 1)		G74 I75 L76 H113 V130 F132 P133 T134 Y135 K136
Annotation score1
Binding affinityMOAD: Kd=154uM
PDBbind-CN: -logKd/Ki=3.81,Kd=154uM
BindingDB: IC50=149000nM,Kd=154000nM
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:2hu6, PDBe:2hu6, PDBj:2hu6
PDBsum2hu6
PubMed16899369
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

[Back to BioLiP]