Structure of PDB 3ts4 Chain A

Receptor sequence

>3ts4A (length=159) Species: 9606 (Homo sapiens)

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG

3D structure

• PDB: 3ts4 Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.
• Chain: A
• Resolution: 1.587 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H114 E115 H118 H124
• 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	H114 H118 H124
BS02	ZN	A	H168 D170 H183 H196	H64 D66 H79 H92
BS03	CA	A	D158 G190 G192 D194	D54 G86 G88 D90
BS04	CA	A	D124 E199 E201	D20 E95 E97
BS05	CA	A	D175 G176 G178 I180 D198 E201	D71 G72 G74 I76 D94 E97
BS06	EEG	A	I180 L181 A182 H183 L214 H218 E219 H222 H228 K233 A234 P238 T239 Y240	I76 L77 A78 H79 L110 H114 E115 H118 H124 K129 A130 P134 T135 Y136	MOAD: Ki=1.9nM PDBbind-CN: -logKd/Ki=8.72,Ki=1.9nM BindingDB: Ki=1.92nM

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:3ts4, PDBe:3ts4, PDBj:3ts4
• PDBsum: 3ts4
• PubMed: 22689580
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)