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Structure
Human PGAM1, His11-phosphorylated active form 4GPZ (Hitosugi T et al., Nat Commun 2013, PMID:23653202); citrate-bound 1YFK (Wang Y et al., BBRC 2005, PMID:15883004). Note: the scaffold shown in the viewer is 2F90, which is technically the homolog bisphosphoglycerate mutase (BPGM), not PGAM1; the real PGAM1 structures above are the accurate source for the phospho-primed mechanism.
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① Phospho-His11 primed enzyme
His11 is already phosphorylated (phospho-H11), primed by a catalytic trace of 2,3-BPG — the exact active form captured in 4GPZ (Hitosugi T et al., Nat Commun 2013, PMID:23653202).
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② Relay through phosphohistidine
[schematic] The His11 phosphate lands on the 3-PG C2-OH to form a transient 2,3-BPG intermediate; the C3 phosphate then returns to His11 — a double in-line displacement that regenerates the phospho-enzyme and leaves 2-PG.
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③ 2PG released
[schematic] 2-phosphoglycerate dissociates toward enolase; the equilibrium 3PG ↔ 2PG sits near unity with the phospho-H11 regenerated each cycle.
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Sequence
DNA/gene NCBI Gene 5223 · protein UniProt P18669
› 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.