› 3tqa

X-ray diffraction
2.3Å resolution

Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with NADPH

Released:
DOI: 10.2210/pdb3tqa/pdb
PDB entry 3tqa coloured by chain, front view.
PDB entry 3tqa coloured by chain, side view.
PDB entry 3tqa coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

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-182895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.92 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83AB2 (Residues: 1-161; Coverage: 100%)
Gene names: CBU_1993, folA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21
Unit cell:
a: 49.419Å b: 37.026Å c: 52.989Å
α: 90° β: 108.02° γ: 90°
R-values:
R R work R free
0.25 0.247 0.299
Expression system: Escherichia coli

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Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more