Crystal structure of the catalytic domain of mmp-12 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 17% strand (DSSP).

Ligands and binding sites

• H27 · (2R)-2-[{(E)-2-[({(2R,3R,4R,5S,6R)-3-(acetylamino)-4,5-bis(acetyloxy)-6-[(acetyloxy)methyl]tetrahydro-2H-pyran-2-yl}carbamothioyl)amino]ethenyl}(biphenyl-4-ylsulfonyl)amino]-3-methylbutanoic acid · ligand · 2 copies · chains A, B
• CA · Calcium ion · metal · 6 copies · chains A, B
• ZN · Zinc ion · metal · 4 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
• PGO · S-1,2-propanediol · additive · chains A
• PEG · Di(hydroxyethyl)ether · additive · chains A
• DMS · Dimethyl sulfoxide · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 259 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 5I0L · Crystal structure of the catalytic domain of MMP-12 in complex with a selective… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P39900
• Elsewhere: RCSB PDB 5I0L · PDBe 5I0L · UniProt P39900