› 3ia4

X-ray diffraction
1.7Å resolution

Moritella profunda dihydrofolate reductase (DHFR) in complex with NADPH and methotrexate (MTX)

Released:
DOI: 10.2210/pdb3ia4/pdb
PDB entry 3ia4 coloured by chain, front view.
PDB entry 3ia4 coloured by chain, side view.
PDB entry 3ia4 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, C, D
Molecule details ›
Chains: A, B, C, D
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


Cofactor: Ligand NDP 4 x NDP
1 bound ligand:
Ligand MTX 4 x MTX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 183.87Å b: 44.99Å c: 97.37Å
α: 90° β: 114.82° γ: 90°
R-values:
R R work R free
0.157 0.154 0.199
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

4 mentions without citation

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