› 2d0k

X-ray diffraction
1.9Å resolution

Methionine-free mutant of Escherichia coli dihydrofolate reductase

Released:
DOI: 10.2210/pdb2d0k/pdb
PDB entry 2d0k coloured by chain, front view.
PDB entry 2d0k coloured by chain, side view.
PDB entry 2d0k coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase.
Iwakura M, Maki K, Takahashi H, Takenawa T, Yokota A, Katayanagi K, Kamiyama T, Gekko K
J Biol Chem 281 13234-13246 (2006)
PMID: 16510443

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142189 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.92 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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

2 bound ligands:
Ligand CL 2 x CL
Ligand FOL 2 x FOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: C2
Unit cell:
a: 79.58Å b: 56.69Å c: 85.14Å
α: 90° β: 106.81° γ: 90°
R-values:
R R work R free
0.205 0.205 0.284
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.
Currin et al. (2015)
16 other articles

1 mention without citation

Computational methods for predicting sites of functionally important dynamics.
Schuyler et al. (2009)