Structure of PDB 1jk3 Chain A

Receptor sequence

>1jk3A (length=158) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHAIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG

3D structure

• PDB: 1jk3 Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure.
• Chain: A
• Resolution: 1.09 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 A219 H222 H228
• Catalytic site (residue number reindexed from 1): H113 A114 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	D175 G176 G178 I180 D198 E201	D70 G71 G73 I75 D93 E96
BS04	CA	A	D158 G190 G192 D194	D53 G85 G87 D89
BS05	CA	A	D124 E199 E201	D19 E94 E96
BS06	BAT	A	G179 I180 L181 A182 H218 H222 H228 P238 Y240	G74 I75 L76 A77 H113 H117 H123 P133 Y135

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:1jk3, PDBe:1jk3, PDBj:1jk3
• PDBsum: 1jk3
• PubMed: 11575928
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)