› 4a2r

X-ray diffraction
1.3Å resolution

Structure of the engineered retro-aldolase RA95.5-5

Released:
DOI: 10.2210/pdb4a2r/pdb
PDB entry 4a2r coloured by chain, front view.
PDB entry 4a2r coloured by chain, side view.
PDB entry 4a2r coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Evolution of a designed retro-aldolase leads to complete active site remodeling.
Giger L, Caner S, Obexer R, Kast P, Baker D, Ban N, Hilvert D
OpenAccess logo Nat Chem Biol 9 494-8 (2013)
PMID: 23748672

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 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: 258 amino acids
Theoretical weight: 29.76 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06121 (Residues: 1-245; Coverage: 99%)
Gene names: SSO0895, trpC
Sequence domains: Indole-3-glycerol phosphate synthase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 3NK 1 x 3NK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3121
Unit cell:
a: 53.88Å b: 53.88Å c: 148.61Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.139 0.138 0.165
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

48 review citations

The coming of age of de novo protein design.
Huang et al. (2016)
47 more

5 mentions without citation

Engineering aldolases as biocatalysts.
Windle et al. (2014)
4 more