Human MMP12 in complex with a peg-linked bifunctional L-glutamate motif inhibitor

Structure

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

Ligands and binding sites

• L88 · (4R,22R)-5,21-dioxo-4,22-bis({3-[4-(4-phenylthiophen-2-yl)phenyl]propanoyl}amino)-10,13,16-trioxa-6,20-diazapentacosane-1,25-dioic 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 · 4 copies · chains A
• GOL · Glycerol · additive · 3 copies · chains A
• PGO · S-1,2-propanediol · additive · 2 copies · chains A
• DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
• PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

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

Compared structures

• 4I03 · Human MMP12 in complex with a PEG-linked bifunctional L-glutamate motif 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 4I03 · PDBe 4I03 · UniProt P39900