› 1ra2

X-ray diffraction
1.6Å resolution

DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)

Released:
DOI: 10.2210/pdb1ra2/pdb
PDB entry 1ra2 coloured by chain, front view.
PDB entry 1ra2 coloured by chain, side view.
PDB entry 1ra2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence.
Sawaya MR, Kraut J
Biochemistry 36 586-603 (1997)
PMID: 9012674

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142189 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
Ligand FOL 1 x FOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 74.261Å b: 59.91Å c: 38.957Å
α: 90° β: 107.63° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Escherichia coli

Quick links

Citations

49 review citations

Understanding protein non-folding.
Uversky et al. (2010)
48 more

12 mentions without citation

Thermodynamics and solvent linkage of macromolecule-ligand interactions.
Duff et al. (2015)
11 more