Structure of PDB 2z2d Chain A

Receptor sequence

>2z2dA (length=158) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG

3D structure

• PDB: 2z2d Solution structure of human macrophage elastase (MMP-12) catalytic domain complexed with a gamma-keto butanoic acid inhibitor
• Chain: A
• Resolution: N/A

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H113 E114 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 G178 I180 D198 E201	D70 G73 I75 D93 E96
BS04	CA	A	D158 G190 I191 G192 G193 D194	D53 G85 I86 G87 G88 D89
BS05	CA	A	D124 E199 D200 E201	D19 E94 D95 E96
BS06	HSI	A	I180 L181 A182 L214 H218 F237 P238 Y240 K241 V243	I75 L76 A77 L109 H113 F132 P133 Y135 K136 V138	BindingDB: IC50=200nM

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:2z2d, PDBe:2z2d, PDBj:2z2d
• PDBsum: 2z2d
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)