1FPG

STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY

Summary for 1FPG

DescriptorFRUCTOSE 1,6-BISPHOSPHATASE, MANGANESE (II) ION, 2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE, ... (5 entities in total)
Functional Keywordshydrolase (phosphoric monoester)
Biological sourceSus scrofa (pig)
Total number of polymer chains2
Total molecular weight74568.43
Authors
Villeret, V.,Huang, S.,Zhang, Y.,Lipscomb, W.N. (deposition date: 1994-12-15, release date: 1995-02-27, Last modification date: 2011-07-13)
Primary citation
Villeret, V.,Huang, S.,Zhang, Y.,Lipscomb, W.N.
Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography.
Biochemistry, 34:4307-4315, 1995
PubMed: 7703244 (PDB entries with the same primary citation)
DOI: 10.1021/bi00013a020
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.3 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers110.6%4.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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