wwPDB validation report of PDB entry 5I0L

catalytic domain of MMP-12 with F171D mutation.

(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

MME,Macrophage elastase,hME,Matrix metalloproteinase-12,MMP-12

Same protein. The inhibitor is an glycoconjugate of the inhibitor in entry 4H84.

Same protein. The glycoconjugate inhibitor in this structure should be compared with the dimeric ligand in entry 4H30.

Macrophage metalloelastase (E.C.3.4.24.65)
Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).

The largest off-origin peak in the Patterson function is 10.33% of the height of the origin peak. No significant pseudotranslation is detected.

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures

20191225.v01 (using entries in the PDB archive December 25th 2019)