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

Structure

x-ray diffraction · 2 distinct chains · 24% 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 · 4 copies · chains A, B, C, D
• PGO · S-1,2-propanediol · additive · 2 copies · chains A
• DMS · Dimethyl sulfoxide · additive · chains A
• GOL · Glycerol · additive · chains B

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

Pockets

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

Interfaces

3 interfaces between chains.

• C–D · 365 Ų buried · 1 hydrogen bond · protein-protein
• A–B · 342 Ų buried · 5 hydrogen bonds · protein-protein
• B–C · 309 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 4H49 · Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor. · 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 4H49 · PDBe 4H49 · UniProt P39900