› 4h49

X-ray diffraction
2.16Å resolution

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

Released:
DOI: 10.2210/pdb4h49/pdb
PDB entry 4h49 coloured by chain, front view.
PDB entry 4h49 coloured by chain, side view.
PDB entry 4h49 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallization of bi-functional ligand protein complexes.
Antoni C, Vera L, Devel L, Catalani MP, Czarny B, Cassar-Lajeunesse E, Nuti E, Rossello A, Dive V, Stura EA
J Struct Biol 182 246-54 (2013)
PMID: 23567804

Function and Biology Details

Reaction catalysed: 
Hydrolysis of soluble and insoluble elastin (1). Specific cleavages are also produced at -Ala(14)-|-Leu- and -Tyr(16)-|-Leu- in the B chain of insulin (2).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153975 (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: 17.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

7 bound ligands:
Ligand ZN 8 x ZN
Ligand CA 12 x CA
Ligand PGO 2 x PGO
Ligand DMS 1 x DMS
Ligand PEG 4 x PEG
Ligand L29 2 x L29
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 47.44Å b: 106.49Å c: 65.88Å
α: 90° β: 94.96° γ: 90°
R-values:
R R work R free
0.17 0.167 0.241
Expression system: Escherichia coli BL21

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Citations

2 review citations

Small Molecule Agents Targeting PD-1 Checkpoint Pathway for Cancer Immunotherapy: Mechanisms of Action and Other Considerations for Their Advanced Development.
Sasikumar et al. (2022)
1 more

2 mentions without citation

Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities.
Boon et al. (2016)
1 more