› 1ufo

X-ray diffraction
1.6Å resolution

Crystal Structure of TT1662 from Thermus thermophilus

Released:
DOI: 10.2210/pdb1ufo/pdb
PDB entry 1ufo coloured by chain, front view.
PDB entry 1ufo coloured by chain, side view.
PDB entry 1ufo coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of TT1662 from Thermus thermophilus HB8: a member of the alpha/beta hydrolase fold enzymes.
Murayama K, Shirouzu M, Terada T, Kuramitsu S, Yokoyama S
Proteins 58 982-4 (2005)
PMID: 15648092

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160756 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 238 amino acids
Theoretical weight: 26.26 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P83821 (Residues: 1-238; Coverage: 100%)
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P31
Unit cell:
a: 129.857Å b: 129.857Å c: 70.119Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.17 0.207
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families.
Dimitriou et al. (2017)
4 more

5 mentions without citation

Carboxylic ester hydrolases from hyperthermophiles.
Levisson et al. (2009)
4 more