› 3tc6

X-ray diffraction
1.6Å resolution

Crystal Structure of Engineered Protein. Northeast Structural Genomics Consortium Target OR63.

Released:
DOI: 10.2210/pdb3tc6/pdb
PDB entry 3tc6 coloured by chain, front view.
PDB entry 3tc6 coloured by chain, side view.
PDB entry 3tc6 coloured by chain, top view.
Source organism: Saccharolobus solfataricus P2
Primary publication:
Exploration of alternate catalytic mechanisms and optimization strategies for retroaldolase design.
Bjelic S, Kipnis Y, Wang L, Pianowski Z, Vorobiev S, Su M, Seetharaman J, Xiao R, Kornhaber G, Hunt JF, Tong L, Hilvert D, Baker D
J Mol Biol 426 256-71 (2014)
PMID: 24161950

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: 29.65 KDa
Source organism: Saccharolobus solfataricus P2
Expression system: Escherichia coli
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 PO4 4 x PO4
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P3121
Unit cell:
a: 60.933Å b: 60.933Å c: 118.565Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.179 0.198
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Directed Evolution of Protein Catalysts.
Zeymer et al. (2018)
3 more

2 mentions without citation

Exploration of alternate catalytic mechanisms and optimization strategies for retroaldolase design.
Bjelic et al. (2014)
1 more