Structure of PDB 5i4o Chain A

Receptor sequence

>5i4oA (length=156) Species: 9606 (Homo sapiens)

VWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMA
DILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHS
GGTNLFLTAVHQIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRG
IQSLYG

3D structure

• PDB: 5i4o Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors.
• Chain: A
• Resolution: 2.05 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	V28	A	G179 I180 A182 L214 T215 H218 Q219 H222 H228 V235 F237 P238 Y240	G72 I73 A75 L107 T108 H111 Q112 H115 H121 V128 F130 P131 Y133	PDBbind-CN: -logKd/Ki=7.28,IC50=53nM
BS02	ZN	A	H218 H222 H228	H111 H115 H121
BS03	ZN	A	H168 D170 H183 H196	H61 D63 H76 H89
BS04	CA	A	D158 G190 G192 D194	D51 G83 G85 D87
BS05	CA	A	D124 E199 E201	D17 E92 E94
BS06	CA	A	D175 G176 G178 I180 D198 E201	D68 G69 G71 I73 D91 E94

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

External links

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