2H4L: Complex Of PmmPGM WITH RIBOSE 1-Phosphate

Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.
PDB ID: 2H4LDownload
MMDB ID: 40977
PDB Deposition Date: 2006/5/24
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 2H4L: monomeric; determined by author
Molecular Components in 2H4L
Label Count Molecule
Protein (1 molecule)
Phosphomannomutase/phosphoglucomutase(Gene symbol: algC)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB