› 4a29

X-ray diffraction
1.1Å resolution

Structure of the engineered retro-aldolase RA95.0

Released:
DOI: 10.2210/pdb4a29/pdb
PDB entry 4a29 coloured by chain, front view.
PDB entry 4a29 coloured by chain, side view.
PDB entry 4a29 coloured by chain, top view.
Source organism: synthetic construct
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: 29.71 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06121 (Residues: 1-247; Coverage: 100%)
Gene names: SSO0895, trpC
Sequence domains: Indole-3-glycerol phosphate synthase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand 3NK 1 x 3NK
Ligand MLT 1 x MLT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 53.94Å b: 62.59Å c: 79.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.12 0.12 0.137
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

46 review citations

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

7 mentions without citation

Conformational dynamics and enzyme evolution.
Petrović et al. (2018)
6 more