2H4L
Complex of PMM/PGM with ribose 1-phosphate
Summary for 2H4L
| Entry DOI | 10.2210/pdb2h4l/pdb |
| Related | 1K2Y 1K35 1P5D 1P5G 1PCJ 1PCM 2H5A |
| Descriptor | Phosphomannomutase/phosphoglucomutase, 1-O-phosphono-alpha-D-ribofuranose, ZINC ION, ... (4 entities in total) |
| Functional Keywords | protein-ligand complex, slow substrate, ribose 1-phosphate, isomerase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 50753.90 |
| Authors | Beamer, L.J. (deposition date: 2006-05-24, release date: 2006-08-08, Last modification date: 2024-10-09) |
| Primary citation | Regni, C.,Shackelford, G.S.,Beamer, L.J. Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Acta Crystallogr.,Sect.F, 62:722-726, 2006 Cited by PubMed Abstract: 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. PubMed: 16880541DOI: 10.1107/S1744309106025887 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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