Structure of PDB 3uvc Chain A

Receptor sequence

>3uvcA (length=158) Species: 9606 (Homo sapiens) [Search protein sequence]

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHAIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYG

3D structure

PDB

3uvc Characterization of fragments interacting with MMP-12

Chain

Resolution

1.3 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 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)
BS01	ZN	A	H218 H222 H228	H113 H117 H123
BS02	ZN	A	H168 D170 H183 H196	H63 D65 H78 H91
BS03	CA	A	D124 E199 E201	D19 E94 E96
BS04	CA	A	D158 G190 G192 D194	D53 G85 G87 D89
BS05	CA	A	D175 G176 G178 I180 D198 E201	D70 G71 G73 I75 D93 E96
BS06	CA	A	S142 T145	S37 T40
BS07	0D2	A	I180 L181 A182 H218 H222 H228 P238 T239 Y240	I75 L76 A77 H113 H117 H123 P133 T134 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

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:3uvc, PDBe:3uvc, PDBj:3uvc
PDBsum	3uvc
PubMed
UniProt	P39900\|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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