› 7mqp

X-ray diffraction
2.1Å resolution

E. coli dihydrofolate reductase complexed with 4'-chloro-3'-(4-(2,4-diamino-6-ethylpyrimidin-5-yl)but-3-yn-2-yl)-[1,1'-biphenyl]-4-carboxamide (UCP1228)

Released:
DOI: 10.2210/pdb7mqp/pdb
PDB entry 7mqp coloured by chain, front view.
PDB entry 7mqp coloured by chain, side view.
PDB entry 7mqp 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-142197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase

Ligands and Environments

2 bound ligands:
Ligand ZM4 1 x ZM4
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P6122
Unit cell:
a: 66.681Å b: 66.681Å c: 213.752Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.233
Expression system: Escherichia coli BL21(DE3)

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)