Structure of PDB 6ela Chain A

Receptor sequence

>6elaA (length=157) Species: 9606 (Homo sapiens)

PVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM
ADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTH
SGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYAYVDINTFRLSADDIR
GIQSLYG

3D structure

• PDB: 6ela Development of Thioaryl-Based Matrix Metalloproteinase-12 Inhibitors with Alternative Zinc-Binding Groups: Synthesis, Potentiometric, NMR, and Crystallographic Studies.
• Chain: A
• Resolution: 1.485 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H112 E113 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	ZN	A	H218 H222 H228	H112 H116 H122
BS02	ZN	A	H168 D170 H183 H196	H62 D64 H77 H90
BS03	CA	A	D158 G190 G192 D194	D52 G84 G86 D88
BS04	CA	A	D124 E199 E201	D18 E93 E95
BS05	CA	A	D175 G176 G178 I180 D198 E201	D69 G70 G72 I74 D92 E95
BS06	B9Z	A	G179 A182 H218 E219 H222 H228 V235 F237 P238 T239 Y240	G73 A76 H112 E113 H116 H122 V129 F131 P132 T133 Y134	PDBbind-CN: -logKd/Ki=7.59,IC50=26nM BindingDB: IC50=26nM

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