› 1rx4

X-ray diffraction
2.2Å resolution

DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE

Released:
DOI: 10.2210/pdb1rx4/pdb
PDB entry 1rx4 coloured by chain, front view.
PDB entry 1rx4 coloured by chain, side view.
PDB entry 1rx4 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
2 bound ligands:
Ligand DDF 1 x DDF
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 34.923Å b: 45.075Å c: 100.879Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Escherichia coli

Quick links

Citations

45 review citations

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

29 mentions without citation

Flexibility, diversity, and cooperativity: pillars of enzyme catalysis.
Hammes et al. (2011)
28 more