› 2inq

Neutron Diffraction
2.2Å resolution

Neutron Crystal Structure of Escherichia coli Dihydrofolate Reductase Bound to the Anti-cancer drug, Methotrexate

Released:
DOI: 10.2210/pdb2inq/pdb
PDB entry 2inq coloured by chain, front view.
PDB entry 2inq coloured by chain, side view.
PDB entry 2inq coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate.
Bennett B, Langan P, Coates L, Mustyakimov M, Schoenborn B, Howell EE, Dealwis C
Proc Natl Acad Sci U S A 103 18493-8 (2006)
PMID: 17130456

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 domain:

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: 18.02 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
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

2 bound ligands:
Ligand MT1 2 x MT1
Ligand DOD 144 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P61
Unit cell:
a: 93.12Å b: 93.12Å c: 73.87Å α: 90° β: 90° γ: 120°
R-values:
R R work R free not available not available 0.233
Expression system: Escherichia coli

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Citations

2 review citations

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

17 mentions without citation

Neutron crystallography: opportunities, challenges, and limitations.
Blakeley et al. (2008)
16 more