› 1dhi

X-ray diffraction
1.9Å resolution

LONG-RANGE STRUCTURAL EFFECTS IN A SECOND-SITE REVERTANT OF A MUTANT DIHYDROFOLATE REDUCTASE

Released:
DOI: 10.2210/pdb1dhi/pdb
PDB entry 1dhi coloured by chain, front view.
PDB entry 1dhi coloured by chain, side view.
PDB entry 1dhi coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Long-range structural effects in a second-site revertant of a mutant dihydrofolate reductase.
Brown KA, Howell EE, Kraut J
Proc Natl Acad Sci U S A 90 11753-6 (1993)
PMID: 8265622

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.99 KDa
Source organism: Escherichia coli
Expression system: Not provided
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

3 bound ligands:
Ligand CL 2 x CL
Ligand MTX 2 x MTX
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P61
Unit cell:
a: 93.19Å b: 93.19Å c: 73.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

The binding site of aminergic G protein-coupled receptors: the transmembrane segments and second extracellular loop.
Shi et al. (2002)
1 more

2 mentions without citation

The free energy landscape of small molecule unbinding.
Huang et al. (2011)
1 more