› 1d1g

X-ray diffraction
2.1Å resolution

DIHYDROFOLATE REDUCTASE FROM THERMOTOGA MARITIMA

Released:
DOI: 10.2210/pdb1d1g/pdb
PDB entry 1d1g coloured by chain, front view.
PDB entry 1d1g coloured by chain, side view.
PDB entry 1d1g 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


Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
Ligand MTX 2 x MTX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 35.525Å b: 51.419Å c: 52.961Å
α: 94.5° β: 95.31° γ: 110.15°
R-values:
R R work R free
0.196 0.196 0.242
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

6 mentions without citation

On the relationship between thermal stability and catalytic power of enzymes.
Roca et al. (2007)
5 more