Structure of PDB 4gr8 Chain A

Receptor sequence

>4gr8A (length=152) Species: 9606 (Homo sapiens)

KHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADIL
VVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGT
NLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQS
LY

3D structure

• PDB: 4gr8 Molecular determinants of a selective matrix metalloprotease-12 inhibitor: insights from crystallography and thermodynamic studies.
• Chain: A
• Resolution: 1.299 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H108 E109 H112 H118
• 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	H108 H112 H118
BS02	ZN	A	H168 D170 H183 H196	H58 D60 H73 H86
BS03	CA	A	D158 G190 G192 D194	D48 G80 G82 D84
BS04	CA	A	D124 E199 E201	D14 E89 E91
BS05	CA	A	D175 G176 G178 I180 D198 E201	D65 G66 G68 I70 D88 E91
BS06	R4C	A	G179 L181 A182 H183 T215 H218 E219 H222 H228 V235 F237 T239 Y240	G69 L71 A72 H73 T105 H108 E109 H112 H118 V125 F127 T129 Y130	MOAD: Ki=14.7nM PDBbind-CN: -logKd/Ki=7.83,Ki=14.7nM BindingDB: Ki=15nM

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:4gr8, PDBe:4gr8, PDBj:4gr8
• PDBsum: 4gr8
• PubMed: 23343195
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)