› 1rd7

X-ray diffraction
2.6Å resolution

DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE

Released:
DOI: 10.2210/pdb1rd7/pdb
PDB entry 1rd7 coloured by chain, front view.
PDB entry 1rd7 coloured by chain, side view.
PDB entry 1rd7 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

2 bound ligands:
Ligand FOL 2 x FOL
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 49.233Å b: 65.658Å c: 116.926Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.163 not available
Expression system: Escherichia coli

Quick links

Citations

50 review citations

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

5 mentions without citation

Advances in fluorescence labeling strategies for dynamic cellular imaging.
Dean et al. (2014)
4 more