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Structures
E. coli PFK in complex with the reaction products FBP/ADP 1PFK (Shirakihara Y & Evans PR, J Mol Biol 1988, PMID:2975709). Global-framework structure of E. coli PFK 4PFK (Evans PR, Farrants GW & Hudson PJ, Philos Trans R Soc Lond B 1981, PMID:6115424). Human PFKM shares the same ASKHA catalytic machinery.
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① F6P binding
F6P enters its pocket in the real crystal pose; the arginine network (Arg162, Arg171, Arg25) grips the 6-phosphate and Asp127 (general base) aims the 1-OH at the ATP site. F6P pose from 4PFK (Shirakihara Y & Evans PR, J Mol Biol 1988, PMID:2975709).
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② Mg·ATP opposite O1
[schematic] ADP placed where the ATP base sits so the β-P sits ~3.4 Å from the F6P 1-OH on the backside-attack line; Asp127 readies the nucleophile; Mg²⁺ coordinates the γ-phosphate.
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③ Transfer → F1,6BP + ADP
Gamma-phosphate crosses to O1 with inversion in-line; shown by crossfading the real F6P and FBP/ADP product states in 1PFK (reaction-product complex, Shirakihara Y & Evans PR 1988, PMID:2975709).
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④ Release — committed step
Products leave; F1,6BP is handed to aldolase. PFK-1 is the committed, rate-limiting control point; in this structure family allosteric effectors (AMP/F2,6BP activate; ATP/citrate inhibit) tune the ASKHA-active site (framework 4PFK, Evans PR et al., Philos Trans R Soc Lond B 1981, PMID:6115424).
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Sequence
DNA/gene NCBI Gene 5213 · protein UniProt P08237
› Backbones and ligand poses are taken directly from the listed PDB entries,
superposed into one common frame. Where no crystalline state exists for a step
(e.g., Michaelis geometry), the pose is drawn schematically using PubChem 3D
geometries and is labeled as such in the narration.