2PFG
Crystal structure of human CBR1 in complex with BiGF2.
Summary for 2PFG
| Entry DOI | 10.2210/pdb2pfg/pdb |
| Related | 1WMA |
| Descriptor | Carbonyl reductase [NADPH] 1, CHLORIDE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | glutathione, macro molecule, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P16152 |
| Total number of polymer chains | 1 |
| Total formula weight | 31517.08 |
| Authors | Rauh, D.,Bateman, R.L.,Shokat, K.M. (deposition date: 2007-04-04, release date: 2007-09-25, Last modification date: 2023-11-15) |
| Primary citation | Bateman, R.,Rauh, D.,Shokat, K.M. Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct. Org.Biomol.Chem., 5:3363-3367, 2007 Cited by PubMed Abstract: Glutathione forms complex reaction products with formaldehyde, which can be further modified through enzymatic modification. We studied the non-enzymatic reaction between glutathione and formaldehyde and identified a bicyclic complex containing two equivalents of formaldehyde and one glutathione molecule by protein X-ray crystallography (PDB accession number 2PFG). We have also used (1)H, (13)C and 2D NMR spectroscopy to confirm the structure of this unusual adduct. The key feature of this adduct is the involvement of the gamma-glutamyl alpha-amine and the Cys thiol in the formation of the bicyclic ring structure. These findings suggest that the structure of GSH allows for bi-dentate masking of the reactivity of formaldehyde. As this species predominates at near physiological pH values, we suggest this adduct may have biological significance. PubMed: 17912391DOI: 10.1039/b707602a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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