Structure of PDB 6rly Chain A

Receptor sequence

>6rlyA (length=159) Species: 9606 (Homo sapiens)

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG

3D structure

• PDB: 6rly Exploration of zinc-binding groups for the design of inhibitors for the oxytocinase subfamily of M1 aminopeptidases.
• Chain: A
• Resolution: 2.2 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	K8T	A	G179 I180 L181 T215 H218 E219 V235 P238 T239 Y240 K241	G75 I76 L77 T111 H114 E115 V131 P134 T135 Y136 K137	MOAD: Ki=17.5uM

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:6rly, PDBe:6rly, PDBj:6rly
• PDBsum: 6rly
• PubMed: 31711716
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)