› 7r6g

X-ray diffraction
2.61Å resolution

Crystal structure of DfrA5 dihydrofolate reductase in complex with TRIMETHOPRIM and NADPH

Released:
DOI: 10.2210/pdb7r6g/pdb
PDB entry 7r6g coloured by chain, front view.
PDB entry 7r6g coloured by chain, side view.
PDB entry 7r6g coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
Krucinska J, Lombardo MN, Erlandsen H, Estrada A, Si D, Viswanathan K, Wright DL
Commun Biol 5 459 (2022)
PMID: 35562546

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145912 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase type 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 157 amino acids
Theoretical weight: 17.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P11731 (Residues: 1-157; Coverage: 100%)
Gene name: dhfrV
Sequence domains: Dihydrofolate reductase

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand TOP 2 x TOP
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P43
Unit cell:
a: 99.53Å b: 99.53Å c: 42.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.224
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Unveiling the Efficacy of Sesquiterpenes from Marine Sponge Dactylospongia elegans in Inhibiting Dihydrofolate Reductase Using Docking and Molecular Dynamic Studies.
Omar et al. (2023)
1 more

1 mention without citation

Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
Krucinska et al. (2022)