4i03 Summary


Human MMP12 in complex with a PEG-linked bifunctional L-glutamate motif inhibitor

The structure was published by Antoni, C., Vera, L., Devel, L., et al., Rossello, A., Dive, V., and Stura, E.A., in 2013 in a paper entitled "Crystallization of bi-functional ligand protein complexes." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2012.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Macrophage metalloelastase. This molecule has the UniProt identifier P39900 (MMP12_HUMAN)search. The sample contained 159 residues which is < 90% of the natural sequence. Out of 159 residues 159 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Macrophage metalloelastase P39900 (106-263) (MMP12_HUMAN)search Homo sapienssearch < 90% 159 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P39900 (106 - 263) Macrophage metalloelastase Homo sapiens

Chain Sequence family (Pfam)
A Matrixinsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P39900) zinc ion bindingsearch metallopeptidase activitysearch metalloendopeptidase activitysearch extracellular matrixsearch proteolysissearch wound healingsearch

Chain InterPro annotation
A Peptidase M10, metallopeptidasesearch Peptidase, metallopeptidasesearch Peptidase M10Asearch Metallopeptidase, catalytic domainsearch Macrophage metalloelastasesearch