Structure of PDB 5i43 Chain B Binding Site BS01

Receptor Information
>5i43 Chain B (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
THSGGTNLFLTAVHQIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG
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 B Residue 301 [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)		I180 A182 H183 L214 H218 Q219 H222 H228 V235 F237 P238 T239 Y240
Binding residue
(residue number reindexed from 1)		I76 A78 H79 L110 H114 Q115 H118 H124 V131 F133 P134 T135 Y136
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H218 Q219 H222 H228
Catalytic site (residue number reindexed from 1) H114 Q115 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
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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