› 7fq2

X-ray diffraction
1.07Å resolution

DHFR:NADP+:FOL complex at 300 K (multi-crystal)

Released:
DOI: 10.2210/pdb7fq2/pdb
PDB entry 7fq2 coloured by chain, front view.
PDB entry 7fq2 coloured by chain, side view.
PDB entry 7fq2 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism.
Greisman JB, Dalton KM, Brookner DE, Klureza MA, Sheehan CJ, Kim IS, Henning RW, Russi S, Hekstra DR
OpenAccess logo Proc Natl Acad Sci U S A 121 e2313192121 (2024)
PMID: 38386706

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:

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: 18.05 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:
Ligand FOL 1 x FOL
Ligand MN 3 x MN
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-1
Spacegroup: P212121
Unit cell:
a: 34.139Å b: 45.406Å c: 99.036Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.122 0.121 0.144
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Changes in an enzyme ensemble during catalysis observed by high-resolution XFEL crystallography.
Smith et al. (2024)