› 1jom

X-ray diffraction
1.9Å resolution

THE CRYSTAL STRUCTURE OF THE BINARY COMPLEX BETWEEN FOLINIC ACID (LEUCOVORIN) AND E. COLI DIHYDROFOLATE REDUCTASE

Released:
DOI: 10.2210/pdb1jom/pdb
PDB entry 1jom coloured by chain, front view.
PDB entry 1jom coloured by chain, side view.
PDB entry 1jom coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4.
Lee H, Reyes VM, Kraut J
Biochemistry 35 7012-20 (1996)
PMID: 8679526

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: Not provided
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

4 bound ligands:
Ligand CL 1 x CL
Ligand CA 1 x CA
Ligand FFO 1 x FFO
Ligand EOH 3 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P65
Unit cell:
a: 96.862Å b: 96.862Å c: 35.022Å
α: 90° β: 90° γ: 120°
Expression system: Not provided

Quick links

Citations

4 review citations

Binding of small-molecule ligands to proteins: "what you see" is not always "what you get".
Mobley et al. (2009)
3 more

1 mention without citation

The crystal structure of a tetrahydrofolate-bound dihydrofolate reductase reveals the origin of slow product release.
Cao et al. (2018)