4h30 Summary


Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.

A publication describing this structure is not available. The depositing authors are Antoni, C.search; Stura, E.A.search; Vera, L.search; Nuti, E.search; Carafa, L.search; Cassar-Lajeunesse, E.search; Dive, V.search; Rossello, A.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.43 Å and deposited in 2012.

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

This PDB entry contains multiple copies of the structure of Macrophage metalloelastase.

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 most likely forms homodimers.

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%
B 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, B Matrixinsearch

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

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