› 1p89

Solution NMR

Substrate-induced Structural Changes to the Isolated N-Terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase

Released:
DOI: 10.2210/pdb1p89/pdb
PDB entry 1p89 coloured by chain, ensemble of 11 models, front view.
PDB entry 1p89 coloured by chain, ensemble of 11 models, side view.
PDB entry 1p89 coloured by chain, ensemble of 11 models, top view.
Source organism: Escherichia coli O157:H7
Entry authors: Young JK, Stauffer ME, Kim HJ, Helms GL, Evans JNS

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141298 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-phosphoshikimate 1-carboxyvinyltransferase Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.14 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6D3 (Residues: 25-240; Coverage: 51%)
Gene names: JW0891, aroA, b0908
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

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