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

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 17% strand (DSSP).

Ligands and binding sites

• 0XX · N-(4-{[(3R)-3-[(biphenyl-4-ylsulfonyl)(propan-2-yloxy)amino]-4-(hydroxyamino)-4-oxobutyl]amino}-4-oxobutyl)-N'-(4-{[(3S)-3-[(biphenyl-4-ylsulfonyl)(propan-2-yloxy)amino]-4-(hydroxyamino)-4-oxobutyl]amino}-4-oxobutyl)benzene-1,3-dicarboxamide · ligand · 2 copies · chains A, B
• CA · Calcium ion · metal · 7 copies · chains A, B
• ZN · Zinc ion · metal · 4 copies · chains A, B

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.

Interfaces

1 interface between chains.

• A–B · 281 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

• 4H1Q · 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 4H1Q · PDBe 4H1Q · UniProt P14780