Structure of PDB 6eox Chain A

Receptor sequence

>6eoxA (length=158) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG

3D structure

• PDB: 6eox Development of Thioaryl-Based Matrix Metalloproteinase-12 Inhibitors with Alternative Zinc-Binding Groups: Synthesis, Potentiometric, NMR, and Crystallographic Studies.
• Chain: A
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H113 E114 H117 H123
• 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	ZN	A	H218 H222 H228	H113 H117 H123
BS02	ZN	A	H168 D170 H183 H196	H63 D65 H78 H91
BS03	CA	A	D158 G190 G192 D194	D53 G85 G87 D89
BS04	CA	A	D124 E199 E201	D19 E94 E96
BS05	CA	A	D175 G176 G178 I180 D198 E201	D70 G71 G73 I75 D93 E96
BS06	BKW	A	I180 L181 A182 H218 E219 H222 H228 V235 F237 P238 T239 Y240	I75 L76 A77 H113 E114 H117 H123 V130 F132 P133 T134 Y135	PDBbind-CN: -logKd/Ki=6.85,IC50=140nM BindingDB: IC50=140nM

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:6eox, PDBe:6eox, PDBj:6eox
• PDBsum: 6eox
• PubMed: 29727184
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)