› 1cz3

X-ray diffraction
2.1Å resolution

DIHYDROFOLATE REDUCTASE FROM THERMOTOGA MARITIMA

Released:
DOI: 10.2210/pdb1cz3/pdb
PDB entry 1cz3 coloured by chain, front view.
PDB entry 1cz3 coloured by chain, side view.
PDB entry 1cz3 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability.
Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R, Jaenicke R
J Mol Biol 297 659-72 (2000)
PMID: 10731419

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 19.26 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q60034 (Residues: 2-169; Coverage: 99%)
Gene names: TM_1641, dyrA, folA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 131.605Å b: 36.051Å c: 97.025Å
α: 90° β: 130.69° γ: 90°
R-values:
R R work R free
0.203 0.203 0.255
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
3 more

5 mentions without citation

Multiscale simulations of protein landscapes: using coarse-grained models as reference potentials to full explicit models.
Messer et al. (2010)
4 more