› 1vie

X-ray diffraction
1.7Å resolution

STRUCTURE OF DIHYDROFOLATE REDUCTASE

Released:
DOI: 10.2210/pdb1vie/pdb
PDB entry 1vie coloured by chain, front view.
PDB entry 1vie coloured by chain, side view.
PDB entry 1vie coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X
Nat Struct Biol 2 1018-25 (1995)
PMID: 7583655

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase type 2 Chain: A
Molecule details ›
Chain: A
Length: 62 amino acids
Theoretical weight: 6.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00383 (Residues: 17-78; Coverage: 80%)
Sequence domains: R67 dihydrofolate reductase
Structure domains: SH3 type barrels.

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I4122
Unit cell:
a: 68.74Å b: 68.74Å c: 52.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Searching sequence space: two different approaches to dihydrofolate reductase catalysis.
Howell EE. (2005)
2 more

16 mentions without citation

A graph-theory algorithm for rapid protein side-chain prediction.
Canutescu et al. (2003)
15 more