› 5kmq

X-ray diffraction
2.7Å resolution

The structure of I379E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum

Released:
DOI: 10.2210/pdb5kmq/pdb
PDB 5kmq coloured by chain and viewed from the front.
PDB 5kmq coloured by chain and viewed from the side.
PDB 5kmq coloured by chain and viewed from the top.
Source organism: Caldalkalibacillus thermarum TA2.A1
Primary publication:
The mechanism of catalysis by type-II NADH:quinone oxidoreductases.
Blaza JN, Bridges HR, Aragão D, Dunn EA, Heikal A, Cook GM, Nakatani Y, Hirst J
Sci Rep 7 40165 (2017)
PMID: 28067272

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyr_redox_2 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 405 amino acids
Theoretical weight: 44.59 KDa
Source organism: Caldalkalibacillus thermarum TA2.A1
Expression system: Escherichia coli
UniProt:
  • Canonical: F5L3B8 (Residues: 1-399; Coverage: 100%)
Gene name: CathTA2_0279
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

1 bound ligand:
Ligand FAD 4 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 72.383Å b: 114.366Å c: 130.462Å
α: 90° β: 92.04° γ: 90°
R-values:
R R work R free
0.225 0.223 0.269
Expression system: Escherichia coli

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Citations

1 review citation

Recent advances and perspectives in the design and development of polymyxins.
Rabanal et al. (2017)
12 other articles