Crystal structure of mutant mmp-9 catalytic domain in complex with a twin inhibitor.

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 17% strand (DSSP).

Ligands and binding sites

• L29 · N,N'-bis(2-{(biphenyl-4-ylsulfonyl)[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino}ethyl)benzene-1,3-dicarboxamide (non-preferred name) · ligand · 2 copies · chains A, B, C, D
• CA · Calcium ion · metal · 12 copies · chains A, B, C, D
• ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
• PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains C, D
• PGO · S-1,2-propanediol · additive · 3 copies · chains C, D
• PPI · Propanoic acid · additive · chains C
• GOL · Glycerol · additive · chains C

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

Pockets

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

Interfaces

3 interfaces between chains.

• B–C · 312 Ų buried · 3 hydrogen bonds · protein-protein
• C–D · 215 Ų buried · 2 hydrogen bonds · protein-protein
• A–B · 205 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 4H82 · Crystal structure of mutant MMP-9 catalytic domain in complex with a twin inhibitor. · 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 0.97

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 4H82 · PDBe 4H82 · UniProt P14780