› 1ub3

X-ray diffraction
1.4Å resolution

Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1ub3/pdb
PDB entry 1ub3 coloured by chain, front view.
PDB entry 1ub3 coloured by chain, side view.
PDB entry 1ub3 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.
Lokanath NK, Shiromizu I, Ohshima N, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N
Acta Crystallogr D Biol Crystallogr 60 1816-23 (2004)
PMID: 15388928

Function and Biology Details

Reaction catalysed: 
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyribose-phosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 23.34 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJ28 (Residues: 1-220; Coverage: 100%)
Gene names: TTHA1186, deoC
Sequence domains: DeoC/LacD family aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand HPD 4 x HPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 63.82Å b: 96.887Å c: 137.925Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

2-Deoxy-D-ribose-5-phosphate aldolase (DERA): applications and modifications.
Haridas et al. (2018)
1 more

2 mentions without citation

Nanoscale dewetting transition in protein complex folding.
Hua et al. (2007)
1 more