Structure of PDB 5l7f Chain B

Receptor sequence

>5l7fB (length=158) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYAYVDINTFRLSADDI
RGIQSLYG

3D structure

• PDB: 5l7f Synthesis and in Vitro and in Vivo Evaluation of MMP-12 Selective Optical Probes.
• Chain: B
• Resolution: 1.8 Å

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	R47	B	S230 P232	S125 P127	BindingDB: Ki=0.260000nM
BS02	6PJ	B	P232 K233 T247 F248 R249 S251 A252	P127 K128 T142 F143 R144 S146 A147
BS03	ZN	B	H218 H222 H228	H113 H117 H123
BS04	ZN	B	H168 D170 H183 H196	H63 D65 H78 H91
BS05	CA	B	D175 G176 G178 I180 D198 E201	D70 G71 G73 I75 D93 E96
BS06	CA	B	D158 G190 G192 D194	D53 G85 G87 D89
BS07	CA	B	D124 E199 E201	D19 E94 E96
BS08	R47	B	G179 I180 L181 A182 T215 H218 E219 H222 H228 K233 A234 V235 F237 T239 Y240 A241 V243	G74 I75 L76 A77 T110 H113 E114 H117 H123 K128 A129 V130 F132 T134 Y135 A136 V138	BindingDB: Ki=0.260000nM

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:5l7f, PDBe:5l7f, PDBj:5l7f
• PDBsum: 5l7f
• PubMed: 27564088
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)