› 1g81

X-ray diffraction
1.71Å resolution

CHORISMATE LYASE WITH BOUND PRODUCT, ORTHORHOMBIC CRYSTAL FORM

Released:
DOI: 10.2210/pdb1g81/pdb
PDB entry 1g81 coloured by chain, front view.
PDB entry 1g81 coloured by chain, side view.
PDB entry 1g81 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of chorismate lyase shows a new fold and a tightly retained product.
Gallagher DT, Mayhew M, Holden MJ, Howard A, Kim KJ, Vilker VL
Proteins 44 304-11 (2001)
PMID: 11455603

Function and Biology Details

Reaction catalysed: 
Chorismate = 4-hydroxybenzoate + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate pyruvate-lyase Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.65 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P26602 (Residues: 2-165; Coverage: 99%)
Gene names: JW5713, b4039, ubiC
Sequence domains: Chorismate lyase
Structure domains: Chorismate lyase-like

Ligands and Environments

1 bound ligand:
Ligand PHB 1 x PHB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 31.962Å b: 62.983Å c: 71.894Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.202 0.253
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Challenges in enzyme mechanism and energetics.
Kraut et al. (2003)
1 more

1 mention without citation

Docking-based long timescale simulation of cell-size protein systems at atomic resolution.
Vakser et al. (2022)