› 1re7

X-ray diffraction
2.6Å resolution

DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE

Released:
DOI: 10.2210/pdb1re7/pdb
PDB entry 1re7 coloured by chain, front view.
PDB entry 1re7 coloured by chain, side view.
PDB entry 1re7 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand FOL 2 x FOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 44.384Å b: 60.911Å c: 121.971Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 not available
Expression system: Escherichia coli

Quick links

Citations

49 review citations

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

3 mentions without citation

Harnessing Conformational Plasticity to Generate Designer Enzymes.
Crean et al. (2020)
2 more