Crystal structure of the catalytic domain of mmp-9 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).

Structure

x-ray diffraction · 1 distinct chain · 25% 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 · chains A
• CA · Calcium ion · metal · 3 copies · chains A
• ZN · Zinc ion · metal · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · chains A
• DMS · Dimethyl sulfoxide · additive · chains A
• GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 5I12 · Crystal structure of the catalytic domain of MMP-9 in complex with a selective… · the same entry in another collection · chain A against A, TM-score 1.00
• P14780 · AlphaFold monomer V2.0 prediction for matrix metalloproteinase-9 (P14780) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P14780
• Elsewhere: RCSB PDB 5I12 · PDBe 5I12 · UniProt P14780