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From Proteopedia

1os9, resolution 1.85Å ()
Sites:	, , , , , , , , , , , , , , , , , , , , , , , , , , , , and
Ligands:	,
Gene:	MMP12 OR HME (Homo sapiens)
Activity:	Macrophage elastase, with EC number 3.4.24.65
Related:	1jk3, 1os2
Structural annotation: Resources: CATH : 1Os9A00, 1Os9B00, 1Os9C00, 1Os9D00, 1Os9E00, 1Os9F00 InterPro : Ipr002477, Ipr006026, Ipr006025, Ipr001818, Ipr000585 Pfam : PF00413 SCOP : d1os9a_, d1os9b_, d1os9c_, d1os9d_, d1os9e_, d1os9f_ UniProt : P39900
Functional annotation: Cellular component: proteinaceous extracellular matrix Biological process: cell motility proteolysis metabolic process Molecular function: catalytic activity metalloendopeptidase activity zinc ion binding metallopeptidase activity calcium ion binding peptidase activity macrophage elastase activity metal ion binding hydrolase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Binary enzyme-product complexes of human MMP12

About this Structure

1os9 is a 6 chain structure of Elastase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Elastase

Reference

• Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B. X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases. Angew Chem Int Ed Engl. 2003 Jun 16;42(23):2673-6. PMID:12813751 doi:10.1002/anie.200350957