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5i3m

X-ray diffraction
2.17Å resolution

Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated thiourea-linked carboxylate zinc-chelator water-soluble inhibitor (DC31).

Released:
Model geometry
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Function and Biology Details

Reaction catalysed:
Hydrolysis of soluble and insoluble elastin. Specific cleavages are alsoproduced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain ofinsulin.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-153971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage metalloelastase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 159 amino acids
Theoretical weight: 17.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 63.72Å b: 63.14Å c: 78.92Å
α: 90° β: 103.09° γ: 90°
R-values:
R R work R free
0.208 0.206 0.253
Expression system: Escherichia coli