› 2rk1

X-ray diffraction
1.26Å resolution

DHFR R67 Complexed with NADP and dihydrofolate

Released:
DOI: 10.2210/pdb2rk1/pdb
PDB entry 2rk1 coloured by chain, front view.
PDB entry 2rk1 coloured by chain, side view.
PDB entry 2rk1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of a type II dihydrofolate reductase catalytic ternary complex.
Krahn JM, Jackson MR, DeRose EF, Howell EE, London RE
Biochemistry 46 14878-88 (2007)
PMID: 18052202

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase type 2 Chain: A
Molecule details ›
Chain: A
Length: 62 amino acids
Theoretical weight: 6.73 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P00383 (Residues: 17-78; Coverage: 80%)
Sequence domains: R67 dihydrofolate reductase
Structure domains: SH3 type barrels.

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:
Ligand DHF 1 x DHF
Ligand MRD 3 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I4122
Unit cell:
a: 67.804Å b: 67.804Å c: 52.201Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.124 0.123 0.152

Quick links

Citations

10 citation in other articles

Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis.
Ramanathan et al. (2011)
9 more

13 mentions without citation

Thermodynamics and solvent linkage of macromolecule-ligand interactions.
Duff et al. (2015)
12 more