Structure of PDB 5i4o Chain A Binding Site BS01

Receptor Information
>5i4o Chain A (length=156) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMA
DILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHS
GGTNLFLTAVHQIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRG
IQSLYG
Ligand information
Ligand IDV28
InChIInChI=1S/C28H35N5O9S/c1-16(2)24(28(38)39)33(43(40,41)21-11-9-19(10-12-21)18-7-5-4-6-8-18)14-20-13-32(31-30-20)27-23(29-17(3)35)26(37)25(36)22(15-34)42-27/h4-13,16,22-27,34,36-37H,14-15H2,1-3H3,(H,29,35)(H,38,39)/t22-,23-,24-,25-,26-,27-/m1/s1
InChIKeyKNBZJXWGCBPDHT-ZRRJEQDASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.4CC(C)[C@H](C(=O)O)N(Cc1cn(nn1)[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O)NC(=O)C)S(=O)(=O)c3ccc(cc3)c4ccccc4
OpenEye OEToolkits 2.0.4CC(C)C(C(=O)O)N(Cc1cn(nn1)C2C(C(C(C(O2)CO)O)O)NC(=O)C)S(=O)(=O)c3ccc(cc3)c4ccccc4
CACTVS 3.385CC(C)[CH](N(Cc1cn(nn1)[CH]2O[CH](CO)[CH](O)[CH](O)[CH]2NC(C)=O)[S](=O)(=O)c3ccc(cc3)c4ccccc4)C(O)=O
ACDLabs 12.01O=S(=O)(c1ccc(cc1)c2ccccc2)N(C(C(=O)O)C(C)C)Cc3cn(nn3)C4OC(CO)C(O)C(C4NC(C)=O)O
CACTVS 3.385CC(C)[C@@H](N(Cc1cn(nn1)[C@@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2NC(C)=O)[S](=O)(=O)c3ccc(cc3)c4ccccc4)C(O)=O
FormulaC28 H35 N5 O9 S
NameN-({1-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-1H-1,2,3-triazol-4-yl}methyl)-N-[([1,1'-biphenyl]-4-yl)sulfonyl]-D-valine
ChEMBL
DrugBank
ZINCZINC000584905707
PDB chain5i4o Chain A 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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PDB5i4o Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		G179 I180 A182 L214 T215 H218 Q219 H222 H228 V235 F237 P238 Y240
Binding residue
(residue number reindexed from 1)		G72 I73 A75 L107 T108 H111 Q112 H115 H121 V128 F130 P131 Y133
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.28,IC50=53nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 Q219 H222 H228
Catalytic site (residue number reindexed from 1) H111 Q112 H115 H121
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:5i4o, PDBe:5i4o, PDBj:5i4o
PDBsum5i4o
PubMed27356908
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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