› 1lbl

X-ray diffraction
2.4Å resolution

Crystal structure of indole-3-glycerol phosphate synthase (IGPS) in complex with 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate (CdRP)

Released:
DOI: 10.2210/pdb1lbl/pdb
PDB entry 1lbl coloured by chain, front view.
PDB entry 1lbl coloured by chain, side view.
PDB entry 1lbl coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product.
Hennig M, Darimont BD, Jansonius JN, Kirschner K
J Mol Biol 319 757-66 (2002)
PMID: 12054868

Function and Biology Details

Reaction catalysed: 
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Indole-3-glycerol phosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 28.49 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06121 (Residues: 2-248; Coverage: 100%)
Gene names: SSO0895, trpC
Sequence domains: Indole-3-glycerol phosphate synthase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 137 1 x 137
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-20
Spacegroup: P212121
Unit cell:
a: 57.9Å b: 73.8Å c: 104.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.247
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Macromolecular modeling with rosetta.
Das et al. (2008)
4 more

4 mentions without citation

Unlocking New Reactivities in Enzymes by Iminium Catalysis.
Xu et al. (2022)
3 more