› 4rgc

X-ray diffraction
1.05Å resolution

277K Crystal structure of Escherichia Coli dihydrofolate reductase

Released:
DOI: 10.2210/pdb4rgc/pdb
PDB entry 4rgc coloured by chain, front view.
PDB entry 4rgc coloured by chain, side view.
PDB entry 4rgc coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. MC4100
Primary publication:
Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography.
Wan Q, Bennett BC, Wilson MA, Kovalevsky A, Langan P, Howell EE, Dealwis C
Proc Natl Acad Sci U S A 111 18225-30 (2014)
PMID: 25453083

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165154 (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 str. K-12 substr. MC4100
Expression system: Escherichia coli
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 34.299Å b: 45.521Å c: 98.711Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.109 0.108 0.134
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Neutron protein crystallography: A complementary tool for locating hydrogens in proteins.
O'Dell et al. (2016)
4 more

4 mentions without citation

Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography.
Wan et al. (2014)
3 more