3ix9

X-ray diffraction
1.95Å resolution

Crystal structure of Streptococcus pneumoniae dihydrofolate reductase - Sp9 mutant

Released:

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

Assemblies composition:
homo dimer
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-176224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 22.23 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54801 (Residues: 1-168; Coverage: 100%)
Gene names: SP_1571, dfr, dhfR
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21212
Unit cell:
a: 61.838Å b: 93.639Å c: 71.367Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.274
Expression system: Escherichia coli