BioLiP

Receptor Information

>5i4o Chain C (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 ID

V28

InChI

InChI=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

InChIKey

KNBZJXWGCBPDHT-ZRRJEQDASA-N

SMILES

Software	SMILES
OpenEye OEToolkits 2.0.4	CC(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 2.0.4	CC(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 3.385	CC(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 12.01	O=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 3.385	CC(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

Formula

C28 H35 N5 O9 S

Name

N-({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

PDB chain

5i4o Chain C Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	5i4o Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors.
Resolution	2.05 Å
Binding residue (original residue number in PDB)	I180 A182 L214 T215 H218 Q219 H222 H228 V235 F237 P238 Y240
Binding residue (residue number reindexed from 1)	I73 A75 L107 T108 H111 Q112 H115 H121 V128 F130 P131 Y133
Annotation score	1

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.

	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

PDB	RCSB:5i4o, PDBe:5i4o, PDBj:5i4o
PDBsum	5i4o
PubMed	27356908
UniProt	P39900\|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

[Back to BioLiP]

Structure of PDB 5i4o Chain C Binding Site BS02