Structure of PDB 4h84 Chain A

Receptor sequence

>4h84A (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG

3D structure

PDB

4h84 Crystallization of bi-functional ligand protein complexes.

Chain

Resolution

1.592 Å

3D
structure

Catalytic site residues are labeled in the structure
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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)
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	Y38	A	I180 A182 L214 T215 H218 E219 H222 H228 P238 T239 Y240	I76 A78 L110 T111 H114 E115 H118 H124 P134 T135 Y136
BS07	Y38	A	H172 H183 F185	H68 H79 F81

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:4h84, PDBe:4h84, PDBj:4h84
PDBsum	4h84
PubMed	23567804
UniProt	P39900\|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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