Brand  (β version)

color scheme of protein:


interaction residue:

chain: Hide other chain(s)

Code Name Link
CA Calcium ion
ZN Zinc ion
0ZD N,N'-bis(2-[(biphenyl-4ylsulfonyl)[(2r)-1-hydroxy-3-methyl-1-oxobutan-2-yl]-amino]ethyl)benzene-1,3-dicarboxamide
GOL Glycerol
PEG Di(hydroxyethyl)ether
Code : 4H30
Header : hydrolase/hydrolase inhibitor
Title : Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.
Release Data : 2013-04-24
Compound :
mol_id molecule chains synonym
1 Macrophage metalloelastase A,B MME, Macrophage elastase, ME, hME, Matrix metalloproteinase-12, MMP-12
fragment: Human MMP12 catalytic domain (unp residues 106-263)
mutation: F171D
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:511693)
gene: HME, MMP12
expression_system_strain: BL21
expression_system_vector_type: PLASMID
expression_system_plasmid: PET24A
Authors : Antoni, C., Stura, E.A., Vera, L., Nuti, E., Carafa, L., Cassar-Lajeunesse, E., Dive, V., Rossello, A.
Keywords : divalent inhibitor, carboxylic twin inhibitor, Dimerisation, METZINCIN, Zinc protease, hydrolase-hydrolase inhibtior complex, hydrolase-hydrolase inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 1.43 Å )
Citation :

Crystallization of bi-functional ligand protein complexes.

Antoni, C.,Vera, L.,Devel, L.  et al.
(2013)  J.Struct.Biol.  182 : 246 - 254

PubMed: 23567804
DOI: 10.1016/j.jsb.2013.03.015

Chain : A, B
UniProt : P39900 (MMP12_HUMAN)
Reaction : Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16- Tyr-|-Leu-17 in the B chain of insulin.