Structure of PDB 5l79 Chain A

Receptor sequence

>5l79A (length=159) Species: 9606 (Homo sapiens)

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG

3D structure

• PDB: 5l79 Synthesis and in Vitro and in Vivo Evaluation of MMP-12 Selective Optical Probes.
• Chain: A
• Resolution: 2.07 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	D175 G176 G178 I180 D198 E201	D71 G72 G74 I76 D94 E97
BS04	CA	A	D158 G190 G192 D194	D54 G86 G88 D90
BS05	CA	A	D124 E199 E201	D20 E95 E97
BS06	R47	A	G178 G179 L181 A182 H183 T215 H218 E219 H222 H228 A234 V235 F237 T239 Y240 K241 F248	G74 G75 L77 A78 H79 T111 H114 E115 H118 H124 A130 V131 F133 T135 Y136 K137 F144	BindingDB: Ki=0.260000nM
BS07	6PJ	A	K233 Y240 R249 S251 A252	K129 Y136 R145 S147 A148

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:5l79, PDBe:5l79, PDBj:5l79
• PDBsum: 5l79
• PubMed: 27564088
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)