Structure of PDB 5i43 Chain A Binding Site BS06

Receptor Information
>5i43 Chain A (length=157) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM
ADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTH
SGGTNLFLTAVHQIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIR
GIQSLYG
Ligand information
Ligand ID67M
InChIInChI=1S/C37H47N5O13S/c1-22(2)33(36(47)48)42(56(49,50)30-15-13-28(14-16-30)27-11-8-7-9-12-27)20-29-19-41(40-39-29)17-10-18-51-37-32(38-23(3)43)35(54-26(6)46)34(53-25(5)45)31(55-37)21-52-24(4)44/h7-9,11-16,19,22,31-35,37H,10,17-18,20-21H2,1-6H3,(H,38,43)(H,47,48)/t31-,32-,33-,34-,35-,37-/m1/s1
InChIKeyGRIPTHDAFNBNAB-HTJFLOPLSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.4CC(C)C(C(=O)O)N(Cc1cn(nn1)CCCOC2C(C(C(C(O2)COC(=O)C)OC(=O)C)OC(=O)C)NC(=O)C)S(=O)(=O)c3ccc(cc3)c4ccccc4
OpenEye OEToolkits 2.0.4CC(C)[C@H](C(=O)O)N(Cc1cn(nn1)CCCO[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)COC(=O)C)OC(=O)C)OC(=O)C)NC(=O)C)S(=O)(=O)c3ccc(cc3)c4ccccc4
CACTVS 3.385CC(C)[C@@H](N(Cc1cn(CCCO[C@@H]2O[C@H](COC(C)=O)[C@@H](OC(C)=O)[C@H](OC(C)=O)[C@H]2NC(C)=O)nn1)[S](=O)(=O)c3ccc(cc3)c4ccccc4)C(O)=O
ACDLabs 12.01O=C(NC1C(OC(C(C1OC(C)=O)OC(C)=O)COC(C)=O)OCCCn2cc(nn2)CN(S(=O)(=O)c3ccc(cc3)c4ccccc4)C(C(C)C)C(=O)O)C
CACTVS 3.385CC(C)[CH](N(Cc1cn(CCCO[CH]2O[CH](COC(C)=O)[CH](OC(C)=O)[CH](OC(C)=O)[CH]2NC(C)=O)nn1)[S](=O)(=O)c3ccc(cc3)c4ccccc4)C(O)=O
FormulaC37 H47 N5 O13 S
Name
ChEMBL
DrugBank
ZINCZINC000584904705
PDB chain5i43 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

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PDB5i43 Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		G178 G179 I180 A182 H183 L214 H218 Q219 H222 H228 P238 Y240
Binding residue
(residue number reindexed from 1)		G72 G73 I74 A76 H77 L108 H112 Q113 H116 H122 P132 Y134
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.20,IC50=63nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 Q219 H222 H228
Catalytic site (residue number reindexed from 1) H112 Q113 H116 H122
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
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5i43, PDBe:5i43, PDBj:5i43
PDBsum5i43
PubMed27356908
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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