Structure of PDB 5i3m Chain A

Receptor sequence

>5i3mA (length=157) Species: 9606 (Homo sapiens)

PVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM
ADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTH
SGGTNLFLTAVHQIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIR
GIQSLYG

3D structure

• PDB: 5i3m Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors.
• Chain: A
• Resolution: 2.17 Å

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.

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	67F	A	I180 A182 H183 L214 T215 H218 Q219 H222 H228 F237 P238 T239 Y240	I74 A76 H77 L108 T109 H112 Q113 H116 H122 F131 P132 T133 Y134	PDBbind-CN: -logKd/Ki=7.40,IC50=40nM
BS02	ZN	A	H218 H222 H228	H112 H116 H122
BS03	ZN	A	H168 D170 H183 H196	H62 D64 H77 H90
BS04	CA	A	D158 G190 G192 D194	D52 G84 G86 D88
BS05	CA	A	D124 E199 E201	D18 E93 E95
BS06	CA	A	D175 G176 G178 I180 D198 E201	D69 G70 G72 I74 D92 E95

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:5i3m, PDBe:5i3m, PDBj:5i3m
• PDBsum: 5i3m
• PubMed: 27356908
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)