› 1ujp

X-ray diffraction
1.34Å resolution

Crystal Structure of Tryptophan Synthase A-Subunit From Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1ujp/pdb
PDB entry 1ujp coloured by chain, front view.
PDB entry 1ujp coloured by chain, side view.
PDB entry 1ujp coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry.
Asada Y, Sawano M, Ogasahara K, Nakamura J, Ota M, Kuroishi C, Sugahara M, Yutani K, Kunishima N
J Biochem 138 343-53 (2005)
PMID: 16272128

Function and Biology Details

Reaction catalysed: 
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase alpha chain Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 28.98 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: P16608 (Residues: 1-270; Coverage: 100%)
Gene names: TT_C0729, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21
Unit cell:
a: 42.4Å b: 76.868Å c: 42.774Å
α: 90° β: 115.08° γ: 90°
R-values:
R R work R free
0.204 0.203 0.221
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthase.
Fatmi et al. (2010)
3 more

3 mentions without citation

Identification of ligand templates using local structure alignment for structure-based drug design.
Lee et al. (2012)
2 more