Structure of PDB 3ba0 Chain A

Receptor sequence

>3ba0A (length=365) Species: 9606 (Homo sapiens)

GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRF
FWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLI
SNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDE
RRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLL
QRITKTLKSNSWFGC

3D structure

• PDB: 3ba0 Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12.
• Chain: A
• Resolution: 3.0 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	ZN	A	H222 H228	H117 H123
BS02	ZN	A	H168 D170 H183 H196	H63 D65 H78 H91
BS03	CA	A	D158 G192 D194	D53 G87 D89
BS04	CA	A	D124 E199 E201	D19 E94 E96
BS05	CA	A	D175 G176 K177 G178 I180 D198 E201	D70 G71 K72 G73 I75 D93 E96
BS06	CA	A	D289 E333 D381 D430	D184 E228 D276 D325

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:3ba0, PDBe:3ba0, PDBj:3ba0
• PDBsum: 3ba0
• PubMed: 18465858
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)