› 1dyi

X-ray diffraction
1.9Å resolution

ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE, 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE: MECHANISTIC IMPLICATIONS

Released:
DOI: 10.2210/pdb1dyi/pdb
PDB entry 1dyi coloured by chain, front view.
PDB entry 1dyi coloured by chain, side view.
PDB entry 1dyi coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications.
Reyes VM, Sawaya MR, Brown KA, Kraut J
Biochemistry 34 2710-23 (1995)
PMID: 7873554

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: 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

3 bound ligands:
Ligand CL 2 x CL
Ligand FOL 2 x FOL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P61
Unit cell:
a: 93.066Å b: 93.066Å c: 73.81Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.137 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Keep on moving: discovering and perturbing the conformational dynamics of enzymes.
Bhabha et al. (2015)
2 more

1 mention without citation

HullRad: Fast Calculations of Folded and Disordered Protein and Nucleic Acid Hydrodynamic Properties.
Fleming et al. (2018)