› 3ia5

X-ray diffraction
2.1Å resolution

Moritella profunda dihydrofolate reductase (DHFR)

Released:
DOI: 10.2210/pdb3ia5/pdb
PDB entry 3ia5 coloured by chain, front view.
PDB entry 3ia5 coloured by chain, side view.
PDB entry 3ia5 coloured by chain, top view.
Source organism: Moritella profunda
Primary publication:
Are the catalytic properties of enzymes from piezophilic organisms pressure adapted?
Hay S, Evans RM, Levy C, Loveridge EJ, Wang X, Leys D, Allemann RK, Scrutton NS
Chembiochem 10 2348-53 (2009)
PMID: 19681091

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 162 amino acids
Theoretical weight: 18.31 KDa
Source organism: Moritella profunda
Expression system: Escherichia coli
UniProt:
  • Canonical: Q70YQ6 (Residues: 1-162; Coverage: 100%)
Gene name: dyrA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41
Unit cell:
a: 94.728Å b: 94.728Å c: 45.912Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.246
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Marine biocatalysts: enzymatic features and applications.
Trincone A. (2011)
3 more

1 mention without citation

Antifolate agents: a patent review (2006 - 2010).
Wright et al. (2011)